KpATCC43816 Protein target profile

hydrogenase 4, large subunit

Accession: VK055_4456

Gene: hyfG AIK82999.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3H1X8

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Length 569

Pocket druggability (P2Rank · AlphaFold DB model) 0.887

Direct ligand evidence 0 79 total records

Functional annotation 0 EC 6 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 0.89, FPocket 0.83). Use the 3D pocket comparison to verify whether they identify the same site. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Strong predicted binding pocket FPocket selected-pocket score 0.83. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.89. 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 (%): 29.851 Lower values reduce human off-target concern.
Human E-value: 7.38e-09
Gut microbiome similarity: 11.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 43.59 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 92.12 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) 0.887

Structure A0A0H3H1X8

Pocket Pocket 1

Druggability (FPocket) 0.827

Structure A0A0H3H1X8

Pocket Pocket 3

ColabFold model

P2Rank 0.698 · Pocket 1

FPocket 0.063 · Pocket 17

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 528 / 4744 genomes with a hit

Prevalence 11.1%

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.

MSEEKIGQHYLAALHQAFPGVVLDEAWQTKDQLTITVKVNYLPEVVEFLYYQQGGWLSVLFGNDERKLNGHYAVYYVLSMEQGTKCWITVRVEVDANKPEYPSVTPRVPAAVWGEREVRDMYGLVPVGLPDERRLVLPDDWPDELYPLRKDSMDYRQRPAPTTDAETYEFINELGSKKNNVVPIGPLHVTSDEPGHFRLFVDGENIIDADYRLFYVHRGMEKLAETRMGYNEVTFLSDRVCGICGFAHSTAYTTSVENAMGIVVPERAQMIRAILLEVERLHSHLLNLGLACHFTGFDSGFMQFFRVRETSMKMAEILTGARKTYGLNLIGGIRRDLLKEDMIQTRQLAQQMRRDVQELVDMLLSTPNIEQRTVGIGRLDPEIARDFSNVGPMVRASGHARDTRADHPFVGYGLLPMEVHSEQGCDVISRLKVRINEVYTALNMIDFGLDNLPGGPLMVEGFTYIPHRFALGFSEAPRGDDIHWSMTGDNQKLYRWRCRAATYANWPTLRYMLRGNTVSDAPLIIGSLDPCYSCTDRMTVVDVRKKKSKVVSYKELERYSIERKNSPLK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0048038 Binding to a quinone, any member of a class of diketones derivable from aromatic compounds by conversion of two CH groups into CO groups with any necessary rearrangement of double bonds.
GO:0008137 Catalysis of the reaction: NADH + ubiquinone + 5 H+(in) = NAD+ + ubiquinol + 4 H+(out).
GO:0016651 Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0016151 Binding to a nickel (Ni) cation.
GO:0051539 Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

21 records

Show feature table

Start	End	DB	Term	Name
180	537	FunFam	G3DSA:1.10.645.10:FF:000004	Hydrogenase 3, large subunit
218	286	Pfam	PF00374	Nickel-dependent hydrogenase
218	286	InterPro	IPR001501	Nickel-dependent hydrogenase, large subunit
14	546	PANTHER	PTHR43485	HYDROGENASE-4 COMPONENT G
2	134	FunFam	G3DSA:3.30.460.80:FF:000003	Formate hydrogenlyase subunit 5
193	537	SUPERFAMILY	SSF56762	HydB/Nqo4-like
193	537	InterPro	IPR029014	[NiFe]-hydrogenase, large subunit
36	152	Pfam	PF00329	Respiratory-chain NADH dehydrogenase, 30 Kd subunit
36	152	InterPro	IPR001268	NADH:ubiquinone oxidoreductase, 30kDa subunit
296	464	Pfam	PF00346	Respiratory-chain NADH dehydrogenase, 49 Kd subunit
296	464	InterPro	IPR001135	NADH-quinone oxidoreductase, subunit D
466	537	Pfam	PF00346	Respiratory-chain NADH dehydrogenase, 49 Kd subunit
466	537	InterPro	IPR001135	NADH-quinone oxidoreductase, subunit D
9	194	SUPERFAMILY	SSF143243	Nqo5-like
9	194	InterPro	IPR037232	NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily
216	227	ProSitePatterns	PS00535	Respiratory chain NADH dehydrogenase 49 Kd subunit signature.
216	227	InterPro	IPR014029	NADH:ubiquinone oxidoreductase, 49kDa subunit, conserved site
2	134	Gene3D	G3DSA:3.30.460.80	NADH:ubiquinone oxidoreductase, 30kDa subunit
2	134	InterPro	IPR037232	NADH:ubiquinone oxidoreductase, 30kDa subunit superfamily
180	537	Gene3D	G3DSA:1.10.645.10	-
180	537	InterPro	IPR029014	[NiFe]-hydrogenase, large subunit

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

0.887

Likely same site as FPocket 3 1.5 Å 16 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.721

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Surrounding area

Pocket 3 P2Rank #3

0.624

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Surrounding area

Pocket 4 P2Rank #4

0.372

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Surrounding area

Pocket 5 P2Rank #5

0.091

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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 #3

0.827

Likely same site as P2Rank 1 1.5 Å 16 shared residues 100% of smaller site

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Surrounding area

Residue sets

UniProt: Binding site:221-221

UniProt: Binding site:241-241

UniProt: Binding site:244-244

UniProt: Binding site:531-531

UniProt: Binding site:534-534

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.698

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Surrounding area

Pocket 2 P2Rank #2

0.49

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Surrounding area

Pocket 3 P2Rank #3

0.399

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Surrounding area

Pocket 4 P2Rank #4

0.388

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Surrounding area

Pocket 5 P2Rank #5

0.352

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Surrounding area

Residue sets

UniProt: Binding site:221-221

UniProt: Binding site:241-241

UniProt: Binding site:244-244

UniProt: Binding site:531-531

UniProt: Binding site:534-534

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_A0A0H3H1X8	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4456	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.

79 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 29 records from similar proteins

Structural ligands 29 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

3PE PDB via homolog 748.1 Da · LogP 12.06 · TPSA 134.4 Open detail RCSB PDB

BCR PDB via homolog Detail RCSB PDB

CDL PDB via homolog Detail RCSB PDB

CPL PDB via homolog Detail RCSB PDB

DCQ 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
3PE RCSB PDB	6RFQ	F2Z626	748.1 Da LogP 12.06 TPSA 134.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OCCN)OC…`
BCR RCSB PDB	6L7O	Q8DJD9	536.9 Da LogP 12.61 TPSA 0.0	2 viol.	✓ Clean	`CC1=C(C(CCC1)(C)C)\C=C\C(=C\C=C\C(=C\C=C\C=C(/C…`
CDL RCSB PDB	5LNK	W5PJ73	1464.1 Da LogP 23.31 TPSA 242.6	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC(…`
CPL RCSB PDB	6RFQ	F2Z626	758.1 Da LogP 10.94 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])OC…`
DCQ RCSB PDB	6I0D	Q56220	322.4 Da LogP 4.49 TPSA 52.6	✓ Ro5	Alert	`CCCCCCCCCCC1=C(C(=O)C(=C(C1=O)OC)OC)C`
DGD RCSB PDB	6KHI	Q8DJD9	949.3 Da LogP 7.61 TPSA 231.1	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
EHZ RCSB PDB	6YJ4	F2Z626	584.7 Da LogP 3.04 TPSA 182.5	2 viol.	✓ Clean	`CCCCCCCCCCC[C@@H](CC(=O)SCCNC(=O)CCNC(=O)[C@@H]…`
FES RCSB PDB	6KHI	Q8DJD9	175.8 Da LogP 1.29 TPSA 0.0	✓ Ro5	✓ Clean	`S1[Fe]S[Fe]1`
HQH RCSB PDB	6Q8O	Q56220	415.6 Da LogP 5.05 TPSA 71.6	1 viol.	✓ Clean	`C/C=C(\C)/[C@@H]([C@H](C)/C=C(\C)/C=C/C/C(=C/CC…`
HQK RCSB PDB	6Q8X	Q56220	364.9 Da LogP 5.24 TPSA 34.9	1 viol.	✓ Clean	`CC(C)(C)c1ccc(cc1)CSC2=C(C(=O)N(N=C2)C(C)(C)C)Cl`
HQW RCSB PDB	6Q8W	Q56220	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`CC1=C(OC(=C(C1=O)C)OC)[C@H]2C/C(=C/C(=C/c3ccc(c…`
LHG RCSB PDB	6KHI	Q8DJD9	723.0 Da LogP 9.89 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@…`
LMG RCSB PDB	6HUM	Q8DJD9	787.2 Da LogP 9.78 TPSA 152.0	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[C@H]1[C@@H]([C…`
LMN RCSB PDB	6RFQ	F2Z626	1005.2 Da LogP -1.68 TPSA 357.1	3 viol.	✓ Clean	`CCCCCCCCCCC(CCCCCCCCCC)(CO[C@@H]1[C@@H]([C@@H](…`
LMT RCSB PDB	6YJ4	F2Z626	510.6 Da LogP -0.45 TPSA 178.5	3 viol.	✓ Clean	`CCCCCCCCCCCCO[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1…`
NFU RCSB PDB	6CFW	Q8U0Z6	195.6 Da LogP -0.25 TPSA 64.7	✓ Ro5	✓ Clean	`C(=O)[Fe](C#N)(C#N)[Ni]`
PC1 RCSB PDB	5LNK	W5PJ73	790.2 Da LogP 12.17 TPSA 111.2	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)([O-])…`
PGT RCSB PDB	6TJV	Q8DJD9	751.0 Da LogP 10.67 TPSA 148.8	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)O[C@@H](COC(=O)CCCCCCCCCC…`
PL9 RCSB PDB	6KHJ	Q8DJD9	749.2 Da LogP 16.57 TPSA 34.1	2 viol.	Alert	`CC1=C(C(=O)C(=CC1=O)CC=C(C)CCC=C(C)CCC=C(C)CCC=…`
PLC RCSB PDB	6RFQ	F2Z626	622.8 Da LogP 8.12 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@H](CO[P@](=O)(O)OCC[N+](C)…`
PNS RCSB PDB	5LNK	W5PJ73	358.4 Da LogP -0.96 TPSA 145.2	1 viol.	✓ Clean	`CC(C)(COP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O`
PQN RCSB PDB	6L7P	Q8DJD9	450.7 Da LogP 9.16 TPSA 34.1	1 viol.	Alert	`CC1=C(C(=O)c2ccccc2C1=O)C\C=C(/C)\CCC[C@H](C)CC…`
PSC RCSB PDB	6Y79	F2Z626	759.1 Da LogP 11.58 TPSA 108.4	2 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OCC[N…`
SMA RCSB PDB	2YBB	Q56220	514.7 Da LogP 6.14 TPSA 87.4	2 viol.	✓ Clean	`C/C=C(\C)/C=C/C=C[C@@H]([C@@H](C)[C@H]([C@@H](C…`
SQD RCSB PDB	6KHI	Q8DJD9	795.1 Da LogP 8.12 TPSA 186.1	3 viol.	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](COC1[C@@H]([C@H]([C…`
T7X RCSB PDB	6RFR	F2Z626	887.1 Da LogP 9.17 TPSA 209.5	4 viol.	✓ Clean	`CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)(O)OC1[C@@…`
UQ1 RCSB PDB	2YBB	Q56220	250.3 Da LogP 2.32 TPSA 52.6	✓ Ro5	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)CC=C(C)C`
UQ9 RCSB PDB	6RFR	F2Z626	795.2 Da LogP 16.13 TPSA 52.6	2 viol.	Alert	`CC1=C(C(=O)C(=C(C1=O)OC)OC)C\C=C(/C)\CC\C=C(/C)…`
ZMP RCSB PDB	6RFQ	F2Z626	568.7 Da LogP 4.07 TPSA 162.3	1 viol.	✓ Clean	`CCCCCCCCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](C(C)(C…`

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
ZINC102191119 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@@H](O)CO…`
ZINC13544781 ZINC	1.000	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…`
ZINC2105913 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])…`
ZINC4025640 ZINC	1.000	397.4 Da LogP 4.66 TPSA 91.8	✓ Ro5	✓ Clean	`COc1oc([C@H]2C/C(=C/C(C)=C/c3ccc([N+](=O)[O-])c…`
ZINC58649551 ZINC	1.000	498.6 Da LogP 3.65 TPSA 148.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](O)CO)…`
ZINC102191158 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC14880758 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@](=O)(O)OC[…`
ZINC14880760 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@](=O)(O)OC[C…`
ZINC53683910 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[…`
ZINC62592202 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@H](O)CO[P@@](=O)(O)OC[C@…`
ZINC62592203 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC62592204 ZINC	0.795	484.6 Da LogP 3.86 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC…`
ZINC96094841 ZINC	0.795	456.5 Da LogP 3.08 TPSA 142.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC(=O)OC[C@@H](O)CO[P@@](=O)(O)OC[C…`
ZINC101154410 ZINC	0.787	383.4 Da LogP 4.36 TPSA 102.8	✓ Ro5	✓ Clean	`CC(/C=C1\CO[C@@H](c2oc(O)c(C)c(=O)c2C)C1)=C\c1c…`
ZINC102190506 ZINC	0.729	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	0.729	467.5 Da LogP 4.25 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)C…`
ZINC36178999 ZINC	0.711	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC36179002 ZINC	0.711	424.5 Da LogP 4.27 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCCCC`
ZINC44830468 ZINC	0.711	346.5 Da LogP 4.93 TPSA 60.7	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C=C/C(C)=C\CCC(O)(O)O)C(C)(C)…`
ZINC95908757 ZINC	0.711	346.5 Da LogP 4.93 TPSA 60.7	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C=C\C(C)=C/CCC(O)(O)O)C(C)(C)…`
ZINC27416437 ZINC	0.708	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	0.708	411.4 Da LogP 2.69 TPSA 134.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](CO[P@@](=O)(O)OCCN)OC(=O)CCC…`
ZINC13543394 ZINC	0.694	455.4 Da LogP 2.15 TPSA 171.7	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](CO[P@@](=O)(O)OC[C@H](N)C(=O)…`
ZINC5820131 ZINC	0.689	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC5820134 ZINC	0.689	368.4 Da LogP 2.71 TPSA 119.4	✓ Ro5	✓ Clean	`CCCCCC(=O)OC[C@H](COP(=O)(O)O)OC(=O)CCCCC`
ZINC13544783 ZINC	0.686	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)…`
ZINC13543439 ZINC	0.667	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	0.667	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…`
ZINC17284934 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C/C(=O)O)C(C)(C)CCC1`
ZINC17284937 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C\C(=O)O)C(C)(C)CCC1`
ZINC22061499 ZINC	0.650	220.4 Da LogP 4.01 TPSA 20.2	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C/CO)C(C)(C)CCC1`
ZINC4430042 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C/C(C)=C/C(=O)O)C(C)(C)CCC1`
ZINC65748979 ZINC	0.650	214.4 Da LogP 4.65 TPSA 0.0	✓ Ro5	✓ Clean	`C#C/C=C(C)/C=C/C1=C(C)CCCC1(C)C`
ZINC8613746 ZINC	0.650	234.3 Da LogP 4.10 TPSA 37.3	✓ Ro5	✓ Clean	`CC1=C(/C=C\C(C)=C\C(=O)O)C(C)(C)CCC1`
ZINC257355159 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257355160 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257355161 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257355162 ZINC	0.648	496.6 Da LogP -1.71 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)…`
ZINC257373326 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC257373327 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC257373328 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC257373329 ZINC	0.648	468.5 Da LogP -2.49 TPSA 195.6	2 viol.	✓ Clean	`CCCCCCCC(=O)OC[C@@H]1O[C@H](O[C@H]2O[C@H](CO)[C…`
ZINC116913009 ZINC	0.645	276.4 Da LogP 4.93 TPSA 34.1	✓ Ro5	Alert	`CCCCCCCCCC1=C(C)C(=O)C(C)=C(C)C1=O`
ZINC3869683 ZINC	0.643	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@H](O)C(=O)NCCC(=O)NCCS`
ZINC3869684 ZINC	0.643	278.4 Da LogP -1.08 TPSA 98.7	✓ Ro5	✓ Clean	`CC(C)(CO)[C@@H](O)C(=O)NCCC(=O)NCCS`
ZINC36079847 ZINC	0.636	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@@H](CO)OC(=O)CCCCCCC`
ZINC8214428 ZINC	0.636	344.5 Da LogP 4.15 TPSA 72.8	✓ Ro5	✓ Clean	`CCCCCCCC(=O)OC[C@H](CO)OC(=O)CCCCCCC`
ZINC100503478 ZINC	0.628	260.4 Da LogP 2.41 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC32840889 ZINC	0.628	316.5 Da LogP 3.97 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCCC(=O)OC[C@@H](O)CO`
ZINC8437478 ZINC	0.628	274.4 Da LogP 2.80 TPSA 66.8	✓ Ro5	✓ Clean	`CCCCCCCCCCCC(=O)OC[C@@H](O)CO`

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 A0A0H3H1X8