KpATCC43816 Protein target profile

thiol reductant ABC exporter, CydD subunit

Accession: VK055_1567

Gene: AIK80187.1 cydD 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GKY7

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Length 588

Pocket druggability (P2Rank · AlphaFold DB model) 0.612

Direct ligand evidence 0 54 total records

Functional annotation 0 EC 8 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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

Main supporting evidence

Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Second pocket predictor agrees P2Rank predicted binding-site probability 0.61. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 4 structural and 0 bioactivity records.

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 (%): 42.424 Lower values reduce human off-target concern.
Human E-value: 3.8e-10
Gut microbiome similarity: 2.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 81.293 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT: 91.32 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) 0.612

Structure A0A0H3GKY7

Pocket Pocket 1

Druggability (FPocket) 0.682

Structure A0A0H3GKY7

Pocket Pocket 16

ColabFold model

P2Rank 0.192 · Pocket 1

FPocket 0.721 · Pocket 45

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 126 / 4744 genomes with a hit

Prevalence 2.7%

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.

MNKTRQQELTRWLKQQSIISRRWLMISRLLGVASGLLIVAQAWFLARILHRMVMENIPATALLLPLTLLVLIFVLRAWVVWLRERVGFQAGQHIRYEIRRQVLDRLQQAGPAWIQGKPAGSWATLILEQIDDMHDYYARYLPQMTLAACVPLLIVITIFPINWAAALILLGTAPLIPLFMALVGMGAADANRRNFQALARLSGHFLDRLRGMETLRIFHRGQAETDNIRDASQDFRQRTMEVLRLAFLSSGVLEFFTSLSIALVAVYFGFSYLGELNFGHYGAGVTLMAGFLTLILAPEFFQPLRDLGTFYHAKAQAVGAADSLKTFMETPLTQVERGEKTLNDNDLISVEARDLVIKSPEGKVLAGPLNFALPAGARVVLVGQSGSGKSSLLNTLLGFLPYEGSLMVNGVELRELDAERWRRLLSWVGQNPQLPAATLRENVLLAWPEASEAQLRLALDKAWVSEFIALLPQGIHTAVGDQAGRLSVGQAQRIAVARALLVPCRLLLLDEPAASLDAHSEQRVMQALIHASSEQTTLLVTHQLEGLADWDDVWVMQDGQIIEQGDYATLARAGGVFSALLAHRQEEI

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 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:0042883 The directed movement of cysteine into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
GO:0055085 The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.
GO:0140359 Primary active transporter characterized by two nucleotide-binding domains and two transmembrane domains. Uses the energy generated from ATP hydrolysis to drive the transport of a substance across a membrane.
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:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
GO:0034040 Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + lipid(in) = ADP + phosphate + lipid(out).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

46 records

Show feature table

Start	End	DB	Term	Name
486	500	ProSitePatterns	PS00211	ABC transporters family signature.
486	500	InterPro	IPR017871	ABC transporter-like, conserved site
25	292	Pfam	PF00664	ABC transporter transmembrane region
25	292	InterPro	IPR011527	ABC transporter type 1, transmembrane domain
29	316	ProSiteProfiles	PS50929	ABC transporter integral membrane type-1 fused domain profile.
29	316	InterPro	IPR011527	ABC transporter type 1, transmembrane domain
245	267	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
273	277	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
342	588	FunFam	G3DSA:3.40.50.300:FF:000980	Cysteine/glutathione ABC transporter permease/ATP-binding protein CydD
21	556	NCBIfam	TIGR02857	thiol reductant ABC exporter subunit CydD
21	556	InterPro	IPR014216	ABC transporter, CydDC cysteine exporter (CydDC-E) family, permease/ATP-binding protein CydD
345	588	Gene3D	G3DSA:3.40.50.300	-
345	588	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
51	580	PANTHER	PTHR24221	ATP-BINDING CASSETTE SUB-FAMILY B
51	580	InterPro	IPR039421	Type 1 protein exporter
167	188	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
351	582	SUPERFAMILY	SSF52540	P-loop containing nucleoside triphosphate hydrolases
351	582	InterPro	IPR027417	P-loop containing nucleoside triphosphate hydrolase
140	161	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
350	583	ProSiteProfiles	PS50893	ATP-binding cassette, ABC transporter-type domain profile.
350	583	InterPro	IPR003439	ABC transporter-like, ATP-binding domain
29	324	CDD	cd18584	ABC_6TM_AarD_CydD
162	166	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
375	560	SMART	SM00382	AAA_5
375	560	InterPro	IPR003593	AAA+ ATPase domain
282	304	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
189	244	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
23	45	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
80	139	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
2	332	FunFam	G3DSA:1.20.1560.10:FF:000039	Cysteine/glutathione ABC transporter permease/ATP-binding protein CydD
245	272	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
11	331	SUPERFAMILY	SSF90123	ABC transporter transmembrane region
11	331	InterPro	IPR036640	ABC transporter type 1, transmembrane domain superfamily
60	82	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
137	159	TMHMM	TMhelix	Region of a membrane-bound protein predicted to be embedded in the membrane.
369	513	Pfam	PF00005	ABC transporter
369	513	InterPro	IPR003439	ABC transporter-like, ATP-binding domain
21	45	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
3	331	Gene3D	G3DSA:1.20.1560.10	ABC transporter type 1, transmembrane domain
3	331	InterPro	IPR036640	ABC transporter type 1, transmembrane domain superfamily
57	79	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
298	588	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
278	297	Phobius	TRANSMEMBRANE	Region of a membrane-bound protein predicted to be embedded in the membrane.
1	20	Phobius	CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
46	56	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
163	185	TMHMM	TMhelix	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

0.612

Likely same site as FPocket 16 4.3 Å 13 shared residues 81% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.238

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Surrounding area

Pocket 3 P2Rank #3

0.218

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Surrounding area

Pocket 4 P2Rank #4

0.142

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Surrounding area

Pocket 5 P2Rank #5

0.071

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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

0.682 Unusual size

Likely same site as P2Rank 1 4.3 Å 13 shared residues 81% 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

0.192

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Surrounding area

Pocket 2 P2Rank #2

0.182

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Surrounding area

Pocket 3 P2Rank #3

0.165

Likely same site as FPocket 45 2.6 Å 10 shared residues 100% of smaller site

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Surrounding area

Pocket 4 P2Rank #4

0.142

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Surrounding area

Pocket 5 P2Rank #5

0.089

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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_A0A0H3GKY7	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_1567	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.

54 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 4 records from similar proteins

Structural ligands 4 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0SA PDB via homolog 512.7 Da · LogP -0.13 · TPSA 169.3 Open detail RCSB PDB

AGS PDB via homolog Detail RCSB PDB

ANP PDB via homolog Detail RCSB PDB

O34 PDB via homolog Detail RCSB PDB

ZINC100053481 ZINC proposed compound · Tanimoto 1.000 Detail ZINC

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
0SA RCSB PDB	4F4C	P34712	512.7 Da LogP -0.13 TPSA 169.3	3 viol.	✓ Clean	`CCCCCCCCCCCS[C@H]1[C@@H]([C@H]([C@@H]([C@H](O1)…`
AGS RCSB PDB	6QUZ	Q9WYC4	523.2 Da LogP -1.51 TPSA 262.1	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
ANP RCSB PDB	3B60	P63359	506.2 Da LogP -2.06 TPSA 281.9	3 viol.	✓ Clean	`c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…`
O34 RCSB PDB	6P6J	Q1RAG2	481.7 Da LogP 2.66 TPSA 114.5	✓ Ro5	✓ Clean	`C[C@@]1(CSC(=N1)C(C)(C)[C@@H]([C@@H]2CS[C@@H](N…`

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
ZINC100053481 ZINC	1.000	484.6 Da LogP -0.91 TPSA 169.3	2 viol.	✓ Clean	`CCCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H…`
ZINC100057932 ZINC	1.000	498.6 Da LogP -0.52 TPSA 169.3	2 viol.	✓ Clean	`CCCCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@…`
ZINC100058001 ZINC	1.000	470.6 Da LogP -1.30 TPSA 169.3	2 viol.	✓ Clean	`CCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H](…`
ZINC100796989 ZINC	1.000	484.6 Da LogP -0.91 TPSA 169.3	2 viol.	✓ Clean	`CCCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H]…`
ZINC14114498 ZINC	1.000	498.6 Da LogP -0.52 TPSA 169.3	2 viol.	✓ Clean	`CCCCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O[C@H]2O[C@H…`
ZINC12360002 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12360703 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC12503599 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OP(=O…`
ZINC16546165 ZINC	0.855	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	0.855	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	0.855	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	0.855	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	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@](=O)(O)OP(=O)…`
ZINC8586020 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC8586021 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](CO[P@@](=O)(O)OP(=O…`
ZINC8586022 ZINC	0.855	427.2 Da LogP -1.75 TPSA 232.6	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](CO[P@@](=O)(O)OP(=…`
ZINC13518964 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC1532515 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC1571045 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC1842158 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@H](O…`
ZINC2046931 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@H](…`
ZINC2126310 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3201891 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@@H](COP(=O)(O)O)[C@@H]…`
ZINC3201893 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3830180 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@@H](COP(=O)(O)O)[C@@H](…`
ZINC3860156 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@@H](…`
ZINC3977897 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](COP(=O)(O)O)[C@@H](O…`
ZINC4806442 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC8613167 ZINC	0.782	347.2 Da LogP -1.86 TPSA 186.1	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(=O)(O)O)[C@H](O…`
ZINC4096224 ZINC	0.768	346.2 Da LogP -1.90 TPSA 191.9	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](N)(=O)O)[C@@…`
ZINC12503850 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141161066 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC141163786 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@](=O)(O)OS(=O)…`
ZINC4228246 ZINC	0.763	427.3 Da LogP -2.04 TPSA 229.4	1 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](CO[P@@](=O)(O)OS(=O…`
ZINC105372833 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC105372837 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@H](O…`
ZINC17107643 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC204538551 ZINC	0.750	345.3 Da LogP -1.93 TPSA 197.6	✓ Ro5	✓ Clean	`Nc1ncnc2c1ncn2[C@@H]1O[C@H](COP(N)(N)=O)[C@@H](…`
ZINC31475423 ZINC	0.738	434.3 Da LogP -2.99 TPSA 238.4	2 viol.	✓ Clean	`Nc1ncnc2c1ncn2[C@H]1O[C@H](CO[P@@](=O)(O)OC(=O)…`
ZINC100056957 ZINC	0.732	336.5 Da LogP 1.66 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C…`
ZINC100759478 ZINC	0.732	308.4 Da LogP 0.88 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCS[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@@H…`
ZINC101659921 ZINC	0.732	308.4 Da LogP 0.88 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCS[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]…`
ZINC16052385 ZINC	0.732	294.4 Da LogP 0.49 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC6845558 ZINC	0.732	308.4 Da LogP 0.88 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H…`
ZINC76945567 ZINC	0.732	308.4 Da LogP 0.88 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCS[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@@…`
ZINC77293255 ZINC	0.732	294.4 Da LogP 0.49 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCS[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@H…`
ZINC77293258 ZINC	0.732	294.4 Da LogP 0.49 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCS[C@@H]1O[C@@H](CO)[C@@H](O)[C@H](O)[C@@…`
ZINC77293261 ZINC	0.732	294.4 Da LogP 0.49 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCS[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H…`
ZINC85479681 ZINC	0.732	308.4 Da LogP 0.88 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCS[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]…`
ZINC97943321 ZINC	0.732	308.4 Da LogP 0.88 TPSA 90.2	✓ Ro5	✓ Clean	`CCCCCCCCS[C@@H]1O[C@H](CO)[C@H](O)[C@@H](O)[C@H…`

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 A0A0H3GKY7