KpATCC43816 Protein target profile

HAD ATPase, P-type, IC family protein

Accession: VK055_1741

Gene: AIK80361.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A2L0KHL4

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Length 895

Pocket druggability (P2Rank · AlphaFold DB model) 0.705

Direct ligand evidence 0 78 total records

Functional annotation 0 EC 14 GO

Target summary

Promising target candidate with multiple supporting evidence streams.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Independent pocket support: P2Rank + FPocket Both predictors report a high-scoring binding site (P2Rank 0.70, FPocket 0.86). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.86. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.70. Structure available AlphaFold DB model + ColabFold model Review the complete evidence below

Risks to review

Evidence coverage

Core evidence streams are available for this target.

Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target: Hit
Human identity (%): 45.669 Lower values reduce human off-target concern.
Human E-value: 2.21e-25
Gut microbiome similarity: 1.0% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 38.095 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 86.97 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.705

Structure A0A2L0KHL4

Pocket Pocket 1

Druggability (FPocket) 0.863

Structure A0A2L0KHL4

Pocket Pocket 16

ColabFold model

P2Rank 0.626 · Pocket 1

FPocket 0.843 · Pocket 23

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 49 / 4744 genomes with a hit

Prevalence 1.0%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MNTDKPGAPYYQRSVEETLASVQSSPEGISGTEAATRLQQYGENALPQKPGKPAWLRFIAHFNDVLIYVLLAAALLKAVMGHWIDMAVILAVAVVNALIGFIQESNAEKSLQSIRNMLSSEAVAIRQGNHETIPTTSLVPGDIVVIRAGDRIPADLRVIEAHNLRVEEAILTGESTVVEKTTEPLSGDLPLGDRSNLLFSGTTVSSGAGKGIVVATGGNTELGHINQMMAGIEKHRTPLLVQMDKLGKAIFILILVMMAALFVFSLLFRDMPVSELMLSLISLAVASVPEGLPAIISIILSLGVQAMARQKAIIRKLPTVETLGAMTVICSDKTGTLTMNEMTVKAVITADSVYRVEGDSYEPVGKIHAIDDPTPVTIAPGSLFERYLRTIDLCNDSQLIKEESGLWKITGGPTEGALKVLAAKVTLPPLTSELRSKIPFDSQYKYMSTLYRLGEEEVVLVTGAPDVLFRLCQYQQSDSGLQPLDLPYWEGKIEEYAREGLRMVAAAWKPAAAGQTELTHQDLQQGVILLGVAGMMDPPRPEAITAIADCLQAGIRVKMITGDHPQTAMSIGKMLGIGNAGNAITGRELEVMDDAQLSVAAQQFDIFARTSPEDKFRLVQALQSKKEIVGMTGDGVNDAPALKQADVGVAMGIKGTEVTKEAADMVLTDDNFATIASAVREGRRVYDNLKKTILFVMPTNLAQGLLIVIALLAGNVLPLTPVLILWMNMATSATLSFGLAFEAGEKNIMRRPPRDPKIHVMDGFAIWRVAFVGSMIAVSAFILEAWLQPRGYSPEFIRTVLLQTLVTAQWFYMLNCRVSDGFSLTKGLLANKGIWIVSGVLLLLQLLIIYAPFMQMLFGTTGLPFRYWVITFIIGFAMFLIVELEKPLTRKWRSA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

14 GO

Subcellular localization

Localization: CytoplasmicMembrane

Gene Ontology (GO)

GO:0005524 Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
GO:0005215 Enables the directed movement of substances (such as macromolecules, small molecules, ions) into, out of or within a cell, accross or in between cells.
GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
GO:0016887 Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
GO:0012505 A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0046872 Binding to a metal ion.
GO:0005391 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Na+(in) + K+(out) = ADP + phosphate + Na+(out) + K+(in).
GO:0030007 A homeostatic process involved in the maintenance of a steady state level of potassium ions within a cell.
GO:0006883 A homeostatic process involved in the maintenance of a steady state level of sodium ions within a cell.
GO:1990573 The directed movement of potassium ions from outside of a cell, across the plasma membrane and into the cytosol.
GO:1902600 The directed movement of a proton across a membrane.
GO:0036376 The directed movement of sodium ions from inside of a cell, across the plasma membrane and into the extracellular region.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

83 records

Show feature table

Start	End	DB	Term	Name
604	620	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
604	620	InterPro	IPR001757	P-type ATPase
632	648	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
632	648	InterPro	IPR001757	P-type ATPase
664	689	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
664	689	InterPro	IPR001757	P-type ATPase
489	507	PRINTS	PR00120	H+-transporting ATPase (proton pump) signature
489	507	InterPro	IPR001757	P-type ATPase
885	895	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
80	102	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
531	542	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
553	563	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
656	668	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
632	651	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
330	344	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
167	181	PRINTS	PR00119	P-type cation-transporting ATPase superfamily signature
332	338	ProSitePatterns	PS00154	E1-E2 ATPases phosphorylation site.
332	338	InterPro	IPR018303	P-type ATPase, phosphorylation site
82	102	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
745	764	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
117	310	Pfam	PF00122	E1-E2 ATPase
337	535	SUPERFAMILY	SSF81660	Metal cation-transporting ATPase, ATP-binding domain N
337	535	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
865	884	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	53	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
9	893	SUPERFAMILY	SSF81665	Calcium ATPase, transmembrane domain M
9	893	InterPro	IPR023298	P-type ATPase, transmembrane domain superfamily
280	308	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
28	230	Gene3D	G3DSA:2.70.150.10	-
269	279	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
103	248	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
328	735	SUPERFAMILY	SSF56784	HAD-like
328	735	InterPro	IPR036412	HAD-like superfamily
9	82	SMART	SM00831	Cation_ATPase_N_a_2
9	82	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
312	685	SFLD	SFLDF00027	p-type atpase
312	685	InterPro	IPR044492	P-type ATPase, haloacid dehalogenase domain
120	229	SUPERFAMILY	SSF81653	Calcium ATPase, transduction domain A
120	229	InterPro	IPR008250	P-type ATPase, A domain superfamily
10	76	Pfam	PF00690	Cation transporter/ATPase, N-terminus
10	76	InterPro	IPR004014	Cation-transporting P-type ATPase, N-terminal
283	305	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
865	884	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
340	538	Gene3D	G3DSA:3.40.1110.10	-
340	538	InterPro	IPR023299	P-type ATPase, cytoplasmic domain N
692	714	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
327	339	FunFam	G3DSA:3.40.50.1000:FF:000001	Phospholipid-transporting ATPase IC
828	850	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
719	741	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
764	786	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
784	794	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
693	717	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
326	646	Pfam	PF00702	haloacid dehalogenase-like hydrolase
15	874	PANTHER	PTHR42861	CALCIUM-TRANSPORTING ATPASE
77	81	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
815	833	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
527	677	FunFam	G3DSA:3.40.50.1000:FF:000028	Calcium-transporting P-type ATPase, putative
854	864	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
28	886	CDD	cd02080	P-type_ATPase_cation
718	722	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
795	814	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
60	890	Gene3D	G3DSA:1.20.1110.10	-
104	230	FunFam	G3DSA:2.70.150.10:FF:000160	Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
796	815	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
54	76	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
717	886	Pfam	PF00689	Cation transporting ATPase, C-terminus
717	886	InterPro	IPR006068	Cation-transporting P-type ATPase, C-terminal
233	351	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
233	351	InterPro	IPR001757	P-type ATPase
88	187	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
88	187	InterPro	IPR001757	P-type ATPase
601	725	NCBIfam	TIGR01494	HAD-IC family P-type ATPase
601	725	InterPro	IPR001757	P-type ATPase
327	677	Gene3D	G3DSA:3.40.50.1000	-
327	677	InterPro	IPR023214	HAD superfamily
309	692	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
723	744	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
54	76	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
312	685	SFLD	SFLDG00002	C1.7: P-type atpase like
249	268	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
834	853	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
246	268	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
765	783	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low

How colors and pocket overlays are used

Uniform protein color marks the displayed model as a single molecular object.

Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.

Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.

'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.

'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.

'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.

Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.705

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Surrounding area

Pocket 2 P2Rank #2

0.638

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Surrounding area

Pocket 3 P2Rank #3

0.436

Likely same site as FPocket 16 1.6 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.386

Likely same site as FPocket 62 1.0 Å 12 shared residues 100% of smaller site

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Surrounding area

Pocket 5 P2Rank #5

0.282

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #16

0.863

Likely same site as P2Rank 3 1.6 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #37

0.43

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Surrounding area

Pocket 3 FPocket #62

0.348

Likely same site as P2Rank 4 1.0 Å 12 shared residues 100% of smaller site

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Surrounding area

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1

0.626

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Surrounding area

Pocket 2 P2Rank #2

0.551

Likely same site as FPocket 51 0.7 Å 25 shared residues 100% of smaller site

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Surrounding area

Pocket 3 P2Rank #3

0.395

Likely same site as FPocket 23 1.7 Å 10 shared residues 91% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.342

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Surrounding area

Pocket 5 P2Rank #5

0.335

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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #23

0.843

Likely same site as P2Rank 3 1.7 Å 10 shared residues 91% of smaller site

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Surrounding area

Pocket 2 FPocket #32

0.466

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Surrounding area

Pocket 3 FPocket #51

0.374 Unusual size

Likely same site as P2Rank 2 0.7 Å 25 shared residues 100% of smaller site

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Surrounding area

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold DB AF_A0A2L0KHL4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1741	ColabFold	—	—	full sequence	—	Loaded

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

78 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 28 records from similar proteins

Structural ligands 28 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

128 PDB via homolog 718.3 Da · LogP -1.20 · TPSA 389.7 Open detail RCSB PDB

12D PDB via homolog Detail RCSB PDB

1HT PDB via homolog Detail RCSB PDB

7BL PDB via homolog Detail RCSB PDB

7BS PDB via homolog Detail RCSB PDB

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in Target, use Open crystal to inspect it in the structure viewer.

No PDB structure with a co-crystallized ligand found for this exact protein.

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Ligand	Source crystal	UniProt (homolog)	MW · LogP · TPSA	Lipinski	PAINS	SMILES
128 RCSB PDB	5A3S	P04191-2	718.3 Da LogP -1.20 TPSA 389.7	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
12D RCSB PDB	3AR6	P04191-2	638.3 Da LogP -1.01 TPSA 340.0	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
1HT RCSB PDB	4J2T	P04191-2	720.9 Da LogP 5.28 TPSA 178.0	3 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)C(=C…`
7BL RCSB PDB	4YCN	P04191-2	428.6 Da LogP 6.01 TPSA 55.8	1 viol.	✓ Clean	`C/C=C/C/C(=C\[C@H]1C/C=C/C=C/C[C@@H](/C=C(/[C@H…`
7BS RCSB PDB	4YCM	P04191-2	604.8 Da LogP 4.49 TPSA 123.9	1 viol.	✓ Clean	`C/C=C/C/C(=C\[C@H]1C/C=C/C=C/C[C@@H](/C=C(/[C@H…`
8T8 RCSB PDB	5NCQ	P04191-2	439.3 Da LogP 6.00 TPSA 37.0	1 viol.	Alert	`c1cc(ccc1CN[C@H]2CCCc3c2[nH]c4c3ccc(c4)OC(F)(F)…`
9TN RCSB PDB	2YFY	P04191-2	580.7 Da LogP 2.58 TPSA 165.9	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)/C(=…`
ACP RCSB PDB	6HXB	P11607-2	505.2 Da LogP -1.52 TPSA 269.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ALF RCSB PDB	1XP5	P04191-2	103.0 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al-](F)(F)F`
AN2 RCSB PDB	3BA6	P04191-2	426.2 Da LogP -1.78 TPSA 238.4	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
BEF RCSB PDB	2ZBE	P04191-2	66.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`[Be-](F)(F)F`
BHQ RCSB PDB	2AGV	P04191-2	222.3 Da LogP 3.69 TPSA 40.5	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(c(cc1O)C(C)(C)C)O`
CZA RCSB PDB	5MPM	P11607-2	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`CC(=O)C1=C(N2[C@H](C1=O)[C@H]3c4c[nH]c5c4c(ccc5…`
DBK RCSB PDB	3NAL	B6CAM1	620.8 Da LogP 5.17 TPSA 145.7	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)O[C@H]1C[C@]([C@H]2C[C@H](C(=C2…`
DL5 RCSB PDB	5A3Q	P04191-2	716.3 Da LogP -1.08 TPSA 380.5	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
DMU RCSB PDB	5ZMW	P04191-2	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)C…`
HZ1 RCSB PDB	3NAN	B6CAM1	944.2 Da LogP 7.42 TPSA 230.5	3 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C([C@H]3[C@]([C@H](C[C…`
MF4 RCSB PDB	1WPG	P04191-2	100.3 Da LogP 1.30 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-2](F)(F)F`
MGF RCSB PDB	5MPM	P11607-2	81.3 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Mg-](F)F`
OHW RCSB PDB	6YAA	P04191-2	439.5 Da LogP 4.88 TPSA 40.7	✓ Ro5	Alert	`CCCc1c2ccc(cc2[nH]c1[C@H]3CCCCN3CCN4CCOCC4)OC(F…`
OTK RCSB PDB	3NAM	B6CAM1	510.6 Da LogP 1.98 TPSA 145.7	1 viol.	✓ Clean	`CCCC(=O)O[C@H]1C[C@]([C@H]2C[C@H]([C@@H]([C@H]2…`
PC1 RCSB PDB	2ZBD	P04191-2	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PCW RCSB PDB	4UU1	P04191-2	787.1 Da LogP 12.36 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)…`
PTY RCSB PDB	2AGV	P04191-2	734.1 Da LogP 11.67 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCCCC…`
TBU RCSB PDB	4UU0	P04191-2	74.1 Da LogP 0.78 TPSA 20.2	✓ Ro5	✓ Clean	`CC(C)(C)O`
TG1 RCSB PDB	1IWO	P04191-2	650.8 Da LogP 3.93 TPSA 172.0	2 viol.	✓ Clean	`CCCCCCCC(=O)O[C@H]1[C@H]2C(=C([C@@H]1OC(=O)/C(=…`
TM1 RCSB PDB	3AR8	P04191-2	558.3 Da LogP -1.12 TPSA 293.5	2 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@H]4[C@@H]([C@H](O3)C…`
VN4 RCSB PDB	5A3Q	P04191-2	98.9 Da LogP -1.43 TPSA 57.2	✓ Ro5	✓ Clean	`[O-][V](=O)=O`

Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL bioactivity data found for this exact protein.

Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).

No ChEMBL hits found through similar proteins.

Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).

Ligand	Tanimoto	MW · LogP · TPSA	Lipinski	PAINS	SMILES
ZINC100053689 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC100053691 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC102190506 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCCN)OC(=O)CC…`
ZINC102190512 ZINC	1.000	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC1501015302 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC2039285652 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285653 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285654 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2039285655 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H](C…`
ZINC2053493146 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493147 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493148 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC2053493149 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@H]1O[C@H](CO)[C@H](O[C@@H]2O[C@H]…`
ZINC238809244 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC238809245 ZINC	1.000	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C…`
ZINC252695223 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695224 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695225 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC252695226 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC29084193 ZINC	1.000	336.4 Da LogP 2.83 TPSA 73.4	✓ Ro5	✓ Clean	`CC(=O)C1=C(O)N2[C@H](C1=O)[C@H]1c3c[nH]c4cccc(c…`
ZINC56404 ZINC	1.000	222.3 Da LogP 3.69 TPSA 40.5	✓ Ro5	✓ Clean	`CC(C)(C)c1cc(O)c(C(C)(C)C)cc1O`
ZINC58649715 ZINC	1.000	496.6 Da LogP -0.84 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC59978443 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC66157001 ZINC	1.000	468.5 Da LogP -1.62 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC70669940 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669941 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669942 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC70669943 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@@H](CO)[C@@H](O[C@H]2O[C@…`
ZINC77311968 ZINC	1.000	454.5 Da LogP -2.01 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H]…`
ZINC83433913 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO…`
ZINC85482724 ZINC	1.000	482.6 Da LogP -1.23 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC86002923 ZINC	1.000	426.5 Da LogP -2.79 TPSA 178.5	2 viol.	✓ Clean	`CCCCCCO[C@@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)…`
ZINC27416437 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCCN)OC(=O)CCCCC`
ZINC33902364 ZINC	0.976	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC13544781 ZINC	0.880	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C…`
ZINC13544783 ZINC	0.880	482.6 Da LogP 4.22 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC105469665 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)CP(=O…`
ZINC13527614 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC219330894 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873852 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873853 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC3873854 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)CP(=O)…`
ZINC3873855 ZINC	0.873	425.2 Da LogP -1.64 TPSA 223.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@](=O)(O)CP(=O…`
ZINC13543439 ZINC	0.860	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@](=O)(O)OCC[N+](C)(C)C)…`
ZINC13543441 ZINC	0.860	454.5 Da LogP 3.44 TPSA 108.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)(C)C)O…`
ZINC12503599 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC31977053 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC4806433 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC53683898 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586019 ZINC	0.839	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A2L0KHL4