KpATCC43816 Protein target profile

guanine deaminase

Accession: VK055_0697

Gene: AIK79320.1 guaD 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GQ39

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Length 435

Pocket druggability (P2Rank · AlphaFold DB model) 0.674

Metabolic reactions 3

Chokepoint Yes

Direct ligand evidence 0 56 total records

Functional annotation 1 EC 6 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

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

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 90.5% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Moderate predicted binding pocket FPocket selected-pocket score 0.63. This supports review but is not experimental validation. 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 (%): 37.255 Lower values reduce human off-target concern.
Human E-value: 6.25e-25
Gut microbiome similarity: 1.7% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 0.0 Higher values support similarity to known essential genes.

Structure confidence

ColabFold pLDDT: 96.86 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) 0.674

Structure A0A0H3GQ39

Pocket Pocket 1

Druggability (FPocket) 0.634

Structure A0A0H3GQ39

Pocket Pocket 2

ColabFold model

P2Rank 0.669 · Pocket 1

FPocket 0.714 · Pocket 9

Core conservation Accessory gene

Roary core

CoreCruncher accessory

Gut microbiome 82 / 4744 genomes with a hit

Prevalence 1.7%

Metabolic context

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

Explore metabolic network

Attractive metabolic target: catalyzes a producing & consuming chokepoint reaction in Atrazine degradation, no isoenzyme backup detected, more central than 90.5% of genes in this genome.

Relative network centrality 90.5% more central than 90.5% of genes in this genome

Chokepoint Chokepoint gene

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MDYQTAVRGAFFDIAGVAETPDEVAAQARYLDDGLLFLQEGKIIALLPWQEGEAFLHPLKGYVDLRGKLLLPGFVDTHIHYPQTEMIGAFGEQLLEWLTTYTFPVESQFADAEYAQEIAQFFVNQLISHGTTTALVFCTLHPASVEALFSEALRLNMRLIAGKVMMDRHVPDYLCETAGESYEQTRALIRRWHQRGRLGYAITPRFAPTSTPGLLEAVQRLRAEFPDTWLQTHLSENREEIAWVKQLWPEHARYLDVYHHYQLTGERSVFAHGIHLDDAEWQCLHDTGSAVAFCPTSNLFLGSGLFRLPACWQHQVRMGIGSDVGAGTTFSMLRTLGEAYKVGQLQSYRLRASEAFYHATLGGARALRLEEKIGNFQPGKEADFVVIDPAVTPLQRLRIGRCHDIYEQLFVLMTLGDERNISETWVNGERVWCQD

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Subcellular localization

Localization: Cytoplasmic

Enzyme Commission (EC)

3.5.4.3

Gene Ontology (GO)

GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
GO:0006147 The chemical reactions and pathways resulting in the breakdown of guanine, 2-amino-6-hydroxypurine, a purine that is one of the five main bases found in nucleic acids and a component of a number of phosphorylated guanosine derivatives whose metabolic or regulatory functions are important.
GO:0008892 Catalysis of the reaction: guanine + H2O + H+ = xanthine + NH4+.
GO:0008270 Binding to a zinc ion (Zn).
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
29	428	NCBIfam	TIGR02967	guanine deaminase
29	428	InterPro	IPR014311	Guanine deaminase
30	432	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
30	432	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
19	432	PANTHER	PTHR11271	GUANINE DEAMINASE
70	431	Pfam	PF01979	Amidohydrolase family
70	431	InterPro	IPR006680	Amidohydrolase-related
7	428	CDD	cd01303	GDEase
7	428	InterPro	IPR014311	Guanine deaminase
72	375	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
72	375	InterPro	IPR032466	Metal-dependent hydrolase
73	374	FunFam	G3DSA:3.20.20.140:FF:000022	Guanine deaminase
7	426	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
7	426	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
73	391	Gene3D	G3DSA:3.20.20.140	-

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

0.674

Likely same site as FPocket 1 0.8 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.056

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Surrounding area

Pocket 3 P2Rank #3

0.01

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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

0.634

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Surrounding area

Pocket 2 FPocket #1

0.486

Likely same site as P2Rank 1 0.8 Å 14 shared residues 100% of smaller site

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Surrounding area

Pocket 3 FPocket #6

0.394

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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

0.669

Likely same site as FPocket 2 1.5 Å 11 shared residues 100% of smaller site

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Surrounding area

Pocket 2 P2Rank #2

0.091

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Surrounding area

Pocket 3 P2Rank #3

0.02

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Surrounding area

Pocket 4 P2Rank #4

0.017

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Surrounding area

Pocket 5 P2Rank #5

0.003

Likely same site as FPocket 9 1.8 Å 6 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 #9

0.714

Likely same site as P2Rank 5 1.8 Å 6 shared residues 100% of smaller site

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Surrounding area

Pocket 2 FPocket #4

0.542 Unusual size

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Surrounding area

Pocket 3 FPocket #2

0.444

Likely same site as P2Rank 1 1.5 Å 11 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_A0A0H3GQ39	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_0697	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.

56 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 6 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 3 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

GUN PDB via homolog 151.1 Da · LogP -0.77 · TPSA 100.5 Open detail RCSB PDB

TXC PDB via homolog Detail RCSB PDB

XAN PDB via homolog Detail RCSB PDB

6AP ChEMBL via homolog Detail ChEMBL

CHEMBL1224660 ChEMBL via homolog Detail ChEMBL

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
GUN RCSB PDB	2OOD	Q89NG0	151.1 Da LogP -0.77 TPSA 100.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)C(=O)NC(=N2)N`
TXC RCSB PDB	4AQL	Q9Y2T3	324.3 Da LogP -0.80 TPSA 151.1	✓ Ro5	✓ Clean	`CC(C)[C@@H](C(=O)OCCOCn1cnc2c1N=C(NC2=O)N)N`
XAN RCSB PDB	6OHA	Q07729	152.1 Da LogP -1.06 TPSA 94.4	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)C(=O)NC(=O)N2`

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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
6AP ChEMBL	Q9WTT6	—	150.1 Da LogP -0.48 TPSA 106.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nc(n2)N)N`
CHEMBL1224660 ChEMBL	Q9WTT6	—	179.2 Da LogP -0.29 TPSA 77.7	✓ Ro5	✓ Clean	`CN(C)c1nc(=O)c2[nH]cnc2[nH]1`
CHEMBL321248 ChEMBL	Q9Y2T3	—	166.1 Da LogP -1.05 TPSA 83.5	✓ Ro5	✓ Clean	`Cn1cnc2[nH]c(=O)[nH]c(=O)c21`

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
ZINC1530713 ZINC	1.000	324.3 Da LogP -0.80 TPSA 151.1	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21`
ZINC1851155 ZINC	1.000	324.3 Da LogP -0.80 TPSA 151.1	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21`
ZINC1890104 ZINC	0.849	338.4 Da LogP -0.41 TPSA 151.1	✓ Ro5	✓ Clean	`CC[C@H](C)[C@H](N)C(=O)OCCOCn1cnc2c(=O)[nH]c(N)…`
ZINC22047773 ZINC	0.843	296.3 Da LogP -1.43 TPSA 151.1	✓ Ro5	✓ Clean	`C[C@H](N)C(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21`
ZINC32064000 ZINC	0.782	338.4 Da LogP -0.41 TPSA 151.1	✓ Ro5	✓ Clean	`CC(C)C[C@H](N)C(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21`
ZINC2472817 ZINC	0.750	267.2 Da LogP -0.76 TPSA 125.1	✓ Ro5	✓ Clean	`CC(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21`
ZINC35900202 ZINC	0.741	352.4 Da LogP -1.01 TPSA 154.2	✓ Ro5	✓ Clean	`CC(C)[C@H](NC=O)C(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc…`
ZINC77270545 ZINC	0.741	352.4 Da LogP -0.15 TPSA 137.1	✓ Ro5	✓ Clean	`CCN[C@H](C(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21)C(C)C`
ZINC11616801 ZINC	0.695	354.4 Da LogP -1.44 TPSA 171.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](N)C(=O)OC[C@H](CO)OCn1cnc2c(=O)[nH]…`
ZINC1543916 ZINC	0.695	354.4 Da LogP -1.44 TPSA 171.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)OC[C@@H](CO)OCn1cnc2c(=O)[nH]…`
ZINC1995484 ZINC	0.695	354.4 Da LogP -1.44 TPSA 171.4	✓ Ro5	✓ Clean	`CC(C)[C@H](N)C(=O)OC[C@H](CO)OCn1cnc2c(=O)[nH]c…`
ZINC1530555 ZINC	0.686	225.2 Da LogP -1.33 TPSA 119.0	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCCO)c(=O)[nH]1`
ZINC22052922 ZINC	0.683	424.5 Da LogP 0.77 TPSA 163.4	✓ Ro5	✓ Clean	`CC(C)[C@@H](NC(=O)OC(C)(C)C)C(=O)OCCOCn1cnc2c(=…`
ZINC34391297 ZINC	0.683	424.5 Da LogP 0.77 TPSA 163.4	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)OC(C)(C)C)C(=O)OCCOCn1cnc2c(=O…`
ZINC43463386 ZINC	0.655	261.0 Da LogP 0.54 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2[nH]cnc12`
ZINC4707072 ZINC	0.655	214.0 Da LogP 0.70 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(Br)nc2[nH]cnc12`
ZINC6886310 ZINC	0.655	261.0 Da LogP 0.54 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(I)c2nc[nH]c2n1`
ZINC2569523 ZINC	0.643	305.2 Da LogP -1.21 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCCOP(=O)(O)O)c(=O)[nH]1`
ZINC34036729 ZINC	0.642	458.5 Da LogP 1.17 TPSA 163.4	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)OCc1ccccc1)C(=O)OCCOCn1cnc2c(=…`
ZINC4707332 ZINC	0.625	214.2 Da LogP -1.42 TPSA 140.6	✓ Ro5	✓ Clean	`Nc1nc(S(N)(=O)=O)nc2[nH]cnc12`
ZINC6119301 ZINC	0.596	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COC[C@H](O)CO)c(=O)[nH]1`
ZINC6119302 ZINC	0.596	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COC[C@@H](O)CO)c(=O)[nH]1`
ZINC77293009 ZINC	0.596	285.3 Da LogP -2.00 TPSA 148.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCOC(CO)CO)c(=O)[nH]1`
ZINC13833539 ZINC	0.595	208.2 Da LogP 0.21 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCn1cnc2[nH]c(=O)[nH]c(=O)c21`
ZINC32496999 ZINC	0.594	203.1 Da LogP 0.95 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(C(F)(F)F)c2nc[nH]c2n1`
ZINC5606355 ZINC	0.594	203.1 Da LogP 0.95 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC1505 ZINC	0.571	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COC(CO)CO)c(=O)[nH]1`
ZINC1800215 ZINC	0.567	309.3 Da LogP -0.38 TPSA 128.2	✓ Ro5	✓ Clean	`CC(=O)Nc1nc2c(ncn2COCCOC(C)=O)c(=O)[nH]1`
ZINC1845515 ZINC	0.566	207.2 Da LogP 0.36 TPSA 89.6	✓ Ro5	✓ Clean	`CC(C)Cn1cnc2c(=O)[nH]c(N)nc21`
ZINC1628375 ZINC	0.559	211.2 Da LogP 1.60 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(-c2ccccc2)nc2[nH]cnc12`
ZINC1628378 ZINC	0.559	226.2 Da LogP 1.18 TPSA 106.5	✓ Ro5	✓ Clean	`Nc1ccc(-c2nc(N)c3nc[nH]c3n2)cc1`
ZINC8616088 ZINC	0.559	213.2 Da LogP -0.66 TPSA 114.6	✓ Ro5	✓ Clean	`CS(=O)(=O)c1nc(N)nc2[nH]cnc12`
ZINC22059880 ZINC	0.548	297.3 Da LogP -1.40 TPSA 145.4	✓ Ro5	✓ Clean	`CC(=O)OC[C@@H](CO)OCn1cnc2c(=O)[nH]c(N)nc21`
ZINC22059884 ZINC	0.548	297.3 Da LogP -1.40 TPSA 145.4	✓ Ro5	✓ Clean	`CC(=O)OC[C@H](CO)OCn1cnc2c(=O)[nH]c(N)nc21`
ZINC148164253 ZINC	0.545	209.2 Da LogP -0.65 TPSA 98.8	✓ Ro5	✓ Clean	`COCCn1cnc2c(=O)[nH]c(N)nc21`
ZINC1652244 ZINC	0.545	221.3 Da LogP 0.75 TPSA 89.6	✓ Ro5	✓ Clean	`CC(C)CCn1cnc2c(=O)[nH]c(N)nc21`
ZINC8615379 ZINC	0.543	209.3 Da LogP 1.44 TPSA 80.5	✓ Ro5	✓ Clean	`CC(C)Sc1nc(N)nc2[nH]cnc12`
ZINC91297460 ZINC	0.543	204.2 Da LogP 0.54 TPSA 83.7	✓ Ro5	✓ Clean	`Nc1nc(N2CCCC2)c2nc[nH]c2n1`
ZINC81162221 ZINC	0.537	209.2 Da LogP -1.21 TPSA 126.9	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2CC(=O)O)c(=O)[nH]1`
ZINC1682103 ZINC	0.536	221.3 Da LogP 0.75 TPSA 89.6	✓ Ro5	✓ Clean	`CC[C@H](C)Cn1cnc2c(=O)[nH]c(N)nc21`
ZINC2044665 ZINC	0.536	221.3 Da LogP 0.75 TPSA 89.6	✓ Ro5	✓ Clean	`CC[C@@H](C)Cn1cnc2c(=O)[nH]c(N)nc21`
ZINC2472815 ZINC	0.533	267.2 Da LogP -0.96 TPSA 122.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nc2c(ncn2COCCO)c(=O)[nH]1`
ZINC33981136 ZINC	0.531	311.3 Da LogP -1.01 TPSA 145.4	✓ Ro5	✓ Clean	`CCC(=O)OC[C@@H](CO)OCn1cnc2c(=O)[nH]c(N)nc21`
ZINC33981137 ZINC	0.531	311.3 Da LogP -1.01 TPSA 145.4	✓ Ro5	✓ Clean	`CCC(=O)OC[C@H](CO)OCn1cnc2c(=O)[nH]c(N)nc21`
ZINC1652254 ZINC	0.528	226.2 Da LogP 1.68 TPSA 92.5	✓ Ro5	✓ Clean	`Nc1nc(Nc2ccccc2)c2nc[nH]c2n1`
ZINC3600430 ZINC	0.527	239.2 Da LogP -1.70 TPSA 130.0	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2CC(CO)CO)c(=O)[nH]1`
ZINC1590047 ZINC	0.526	212.2 Da LogP 1.00 TPSA 93.4	✓ Ro5	✓ Clean	`Nc1nc(-c2cccnc2)nc2[nH]cnc12`
ZINC1532183 ZINC	0.517	289.2 Da LogP -1.15 TPSA 156.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2CCOCP(=O)(O)O)c(=O)[nH]1`
ZINC13552969 ZINC	0.514	219.3 Da LogP -0.66 TPSA 95.7	✓ Ro5	✓ Clean	`Nc1nc(N2CCNCC2)c2nc[nH]c2n1`
ZINC17298972 ZINC	0.514	209.3 Da LogP 1.44 TPSA 80.5	✓ Ro5	✓ Clean	`CCCSc1nc(N)nc2[nH]cnc12`

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.

guanine deaminase

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Structure confidence

Binding-site evidence

Metabolic context

Sequence

Functional annotations

Subcellular localization

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Structural evidence

Ligand evidence

Cross-references

Sequence

Chemistry

Pathways