KpATCC43816 Protein target profile

cytidine and deoxycytidylate deaminase zinc-binding region family protein

Accession: VK055_4780

Gene: AIK83308.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A0H3GWF3

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Length 152

Pocket druggability (P2Rank · AlphaFold DB model) 0.657

Direct ligand evidence 0 62 total records

Functional annotation 0 EC 5 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 0.66, FPocket 0.73). Use the 3D pocket comparison to verify whether they identify the same site. Strong predicted binding pocket FPocket selected-pocket score 0.73. This is a computational pocket signal, not binding validation. Second pocket predictor agrees P2Rank predicted binding-site probability 0.66. 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 (%): 26.168 Lower values reduce human off-target concern.
Human E-value: 5.78e-10
Gut microbiome similarity: 0.3% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 41.346 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 97.43 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) 0.657

Structure A0A0H3GWF3

Pocket Pocket 1

Druggability (FPocket) 0.731

Structure A0A0H3GWF3

Pocket Pocket 1

ColabFold model

P2Rank 0.531 · Pocket 1

FPocket 0.302 · Pocket 2

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 16 / 4744 genomes with a hit

Prevalence 0.3%

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.

MSAHDRYLQRALVLAKQNIADGGRPFGAVLVRNDEIVAESVNTFHLSGDPTAHAELNAVRDLAARLGSAVLRECVIYASGQPCPMCLSALYLTGVREVFFANSNQDGEPFQLSTAAIYQQLQQPLAQQTLPIHHRPQPEGTELYQRWAERQS

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

5 GO

Subcellular localization

Localization: Cytoplasmic

Gene Ontology (GO)

GO:0008270 Binding to a zinc ion (Zn).
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0047974 Catalysis of the reaction: guanosine + H2O + H+ = xanthosine + NH4+.
GO:0006152 The chemical reactions and pathways resulting in the breakdown of purine nucleoside, one of a family of organic molecules consisting of a purine base covalently bonded to a sugar ribose (a ribonucleoside) or deoxyribose (a deoxyribonucleoside).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

11 records

Show feature table

Start	End	DB	Term	Name
53	90	ProSitePatterns	PS00903	Cytidine and deoxycytidylate deaminases zinc-binding region signature.
53	90	InterPro	IPR016192	APOBEC/CMP deaminase, zinc-binding
1	101	Pfam	PF00383	Cytidine and deoxycytidylate deaminase zinc-binding region
1	101	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
4	113	PANTHER	PTHR11079	CYTOSINE DEAMINASE FAMILY MEMBER
2	125	ProSiteProfiles	PS51747	Cytidine and deoxycytidylate deaminases domain profile.
2	125	InterPro	IPR002125	Cytidine and deoxycytidylate deaminase domain
2	139	SUPERFAMILY	SSF53927	Cytidine deaminase-like
2	139	InterPro	IPR016193	Cytidine deaminase-like
1	152	Gene3D	G3DSA:3.40.140.10	Cytidine Deaminase, domain 2
8	108	CDD	cd01285	nucleoside_deaminase

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

0.657

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Surrounding area

Pocket 2 P2Rank #2

0.022

Likely same site as FPocket 1 0.9 Å 9 shared residues 100% of smaller site

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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 #1

0.731

Likely same site as P2Rank 2 0.9 Å 9 shared residues 100% of smaller site

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Pocket 1 P2Rank #1

0.531

Likely same site as FPocket 2 6.3 Å 7 shared residues 64% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.114

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Surrounding area

Pocket 3 P2Rank #3

0.026

Likely same site as FPocket 2 2.4 Å 7 shared residues 88% of smaller site

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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 #2

0.302

Likely same site as P2Rank 3 2.4 Å 7 shared residues 88% of smaller site

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Surrounding area

Pocket 2 FPocket #3

0.249

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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_A0A0H3GWF3	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_4780	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.

62 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 12 records from similar proteins

Structural ligands 12 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

5AZ PDB via homolog 112.1 Da · LogP -1.25 · TPSA 84.7 Open detail RCSB PDB

6AM PDB via homolog Detail RCSB PDB

6AP PDB via homolog Detail RCSB PDB

9MG PDB via homolog Detail RCSB PDB

AZG 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
5AZ RCSB PDB	5XKP	A0QY90	112.1 Da LogP -1.25 TPSA 84.7	✓ Ro5	✓ Clean	`C1=NC(=O)NC(=N1)N`
6AM RCSB PDB	5XKQ	A0QY90	127.1 Da LogP -1.26 TPSA 110.9	✓ Ro5	✓ Clean	`c1(nc(nc(n1)O)N)N`
6AP RCSB PDB	4LCP	Q82Y41	150.1 Da LogP -0.48 TPSA 106.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nc(n2)N)N`
9MG RCSB PDB	4LC5	Q82Y41	165.2 Da LogP -0.35 TPSA 89.8	✓ Ro5	✓ Clean	`Cn1cnc2c1nc(nc2O)N`
AZG RCSB PDB	4HRQ	Q82Y41	152.1 Da LogP -0.96 TPSA 113.6	✓ Ro5	✓ Clean	`c12c(nc(nc1O)N)nn[nH]2`
BZE RCSB PDB	5XKR	A0QY90	187.2 Da LogP 0.70 TPSA 90.7	✓ Ro5	✓ Clean	`c1ccc(cc1)c2nc(nc(n2)N)N`
CAC RCSB PDB	5XKO	A0QY90	137.0 Da LogP -0.52 TPSA 40.1	✓ Ro5	✓ Clean	`C[As](=O)(C)[O-]`
CTN RCSB PDB	4LD2	Q82Y41	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`C1=CN(C(=O)N=C1N)[C@H]2[C@@H]([C@@H]([C@H](O2)C…`
CYT RCSB PDB	4LD4	Q82Y41	111.1 Da LogP -0.65 TPSA 71.8	✓ Ro5	✓ Clean	`C1=C(NC(=O)N=C1)N`
DUC RCSB PDB	1UAQ	Q12178	114.1 Da LogP -0.78 TPSA 58.2	✓ Ro5	✓ Clean	`C1CNC(=O)NC1=O`
GNG RCSB PDB	4LCN	Q82Y41	267.2 Da LogP -1.66 TPSA 139.3	✓ Ro5	✓ Clean	`c1nc2c(n1[C@H]3C[C@@H]([C@H](O3)CO)O)NC(=NC2=O)N`
HPY RCSB PDB	1P6O	Q12178	114.1 Da LogP -0.87 TPSA 61.4	✓ Ro5	✓ Clean	`C1=CNC(=O)N[C@H]1O`

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
ZINC1078621 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC12336757 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC12336758 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC16969357 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC2583632 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC3795098 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)…`
ZINC3830623 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)n1`
ZINC3830624 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2O)c(=O)…`
ZINC3978018 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@@H](O)[C@@H]2O)c(=O)n1`
ZINC6091575 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6234828 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC6524892 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@H](O)[C@H]2O)c(=O)n1`
ZINC895248 ZINC	1.000	243.2 Da LogP -2.56 TPSA 130.8	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2O)c(=O)n1`
ZINC1718514 ZINC	0.900	248.3 Da LogP 2.79 TPSA 64.7	✓ Ro5	✓ Clean	`Nc1nc(-c2ccccc2)nc(-c2ccccc2)n1`
ZINC34085615 ZINC	0.829	242.2 Da LogP -2.60 TPSA 136.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2N)c(=O)n1`
ZINC13546396 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@H]2F)c(=O)n1`
ZINC16952044 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@H]2F)c(=O)n1`
ZINC17174505 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@@H]2F)c(=O…`
ZINC17174506 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@@H]2F)c(=O)…`
ZINC2522524 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`
ZINC3817231 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](O)[C@H]2F)c(=O)n1`
ZINC57331 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)…`
ZINC5758597 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@H]2F)c(=O)n1`
ZINC5758598 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O)[C@@H]2F)c(=O)…`
ZINC59201305 ZINC	0.810	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](O)[C@@H]2F)c(=O)n1`
ZINC6524890 ZINC	0.786	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@@H](F)[C@H]2O)c(=O)n1`
ZINC85475812 ZINC	0.786	245.2 Da LogP -1.59 TPSA 110.6	✓ Ro5	✓ Clean	`Nc1ccn([C@@H]2O[C@H](CO)[C@H](F)[C@H]2O)c(=O)n1`
ZINC13546402 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H](O)[C@@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC14953681 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](n2ccc(N)nc2=O)O[C@H](CO)[C@H]1O`
ZINC257373216 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC35635704 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@H](O)[C@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC3806784 ZINC	0.756	252.2 Da LogP -1.78 TPSA 134.4	✓ Ro5	✓ Clean	`N#C[C@H]1[C@H](O)[C@@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC38599713 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](O)[C@@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC4556822 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](n2ccc(N)nc2=O)O[C@@H](CO)[C@H]1O`
ZINC4556823 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H](n2ccc(N)nc2=O)O[C@@H](CO)[C@H]1O`
ZINC4556824 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@@H](O)[C@H](CO)O[C@@H]1n1ccc(N)nc1=O`
ZINC4556825 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](O)[C@H](CO)O[C@@H]1n1ccc(N)nc1=O`
ZINC5998209 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC5998324 ZINC	0.756	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@H](O)[C@@H](CO)O[C@H]1n1ccc(N)nc1=O`
ZINC2288831 ZINC	0.750	296.3 Da LogP -0.28 TPSA 181.4	✓ Ro5	✓ Clean	`Nc1nc(N)nc(-c2ccc(-c3nc(N)nc(N)n3)cc2)n1`
ZINC5541164 ZINC	0.750	435.4 Da LogP -5.38 TPSA 230.2	2 viol.	✓ Clean	`Nc1ccn([C@H]2O[C@@H](CO)[C@@H](O[C@H]3O[C@@H](C…`
ZINC5541165 ZINC	0.750	435.4 Da LogP -5.38 TPSA 230.2	2 viol.	✓ Clean	`Nc1ccn([C@@H]2O[C@@H](CO)[C@@H](O[C@H]3O[C@@H](…`
ZINC1572132 ZINC	0.745	267.2 Da LogP -1.66 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc(=O)[nH]c2c1ncn2[C@H]1C[C@H](O)[C@@H](CO)O1`
ZINC106384020 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@@H](CO)O[C@@H](n2ccc(N)nc2=O)[C@@H]1O`
ZINC106384023 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](O)[C@H](n2ccc(N)nc2=O)O[C@@H]1CO`
ZINC256828171 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](CO)O[C@H](n2ccc(N)nc2=O)[C@H]1O`
ZINC256828175 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](CO)O[C@@H](n2ccc(N)nc2=O)[C@@H]1O`
ZINC256828178 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](CO)O[C@@H](n2ccc(N)nc2=O)[C@H]1O`
ZINC5998228 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@H]1[C@H](O)[C@H](n2ccc(N)nc2=O)O[C@@H]1CO`
ZINC95094424 ZINC	0.733	257.2 Da LogP -1.91 TPSA 119.8	✓ Ro5	✓ Clean	`CO[C@@H]1[C@H](CO)O[C@H](n2ccc(N)nc2=O)[C@@H]1O`

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 A0A0H3GWF3