Protein profile

KP13_05479

Guanine deaminase

Genome: KpKP13

Gene: AHE44484.1 Structure source: AlphaFold + ColabFold UniProt A0A0H3GQ39

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Amino acids 436

Annotations 7

Features 15

PDB binders 3

Druggability 0.634

Overview

Basic information about this protein and its source genome.

Accession: KP13_05479
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE44484.1
Status: annotated
Amino acids: 436
Structure source: AlphaFold + ColabFold

3.5.4.3

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:0008892 Catalysis of the reaction: guanine + H2O + H+ = xanthine + NH4+. 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:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 37.255
Human E-value: 4.05e-25
Gut microbiome off-target: hit
Essential (DEG): N
DEG identity (%): 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 96.86

Selected Druggability evidence

AlphaFold / UniProt model

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.634

Structure A0A0H3GQ39

Pocket Pocket 2

P2Rank 0.674

Structure A0A0H3GQ39

Pocket Pocket 1

ColabFold model

FPocket 0.571 · Pocket 3

P2Rank 0.669 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 82 / 4744 genomes with a hit

Normalized 0.017

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

3.5.4.3

Gene Ontology (GO)

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:0008892 Catalysis of the reaction: guanine + H2O + H+ = xanthine + NH4+.
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:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence Features

Domain/signature hits from InterPro and related databases.

15 records

Show feature table

Start	End	DB	Term	Name
31	433	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
31	433	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
8	429	CDD	cd01303	GDEase
8	429	InterPro	IPR014311	Guanine deaminase
73	376	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
73	376	InterPro	IPR032466	Metal-dependent hydrolase
28	433	PANTHER	PTHR11271	GUANINE DEAMINASE
71	432	Pfam	PF01979	Amidohydrolase family
71	432	InterPro	IPR006680	Amidohydrolase-related
8	427	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
8	427	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
74	392	Gene3D	G3DSA:3.20.20.140	-
74	375	FunFam	G3DSA:3.20.20.140:FF:000022	Guanine deaminase
30	429	NCBIfam	TIGR02967	guanine deaminase
30	429	InterPro	IPR014311	Guanine deaminase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

Loading 3D structure...

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Structural evidence

0 + 2

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry	Method	Resolution	Chain	Coverage	Links	Status
AlphaFold AF_A0A0H3GQ39	AlphaFold	—	—	full sequence	—	Viewing
ColabFold KP13_05479	ColabFold	—	—	full sequence	—	Loaded

Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
2				0.634
5				0.009
19				0.001
10				0.0

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	15.47	0.674
2	2.5	0.056
3	1.23	0.01

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET	Sticks	Spheres	Surfaces	Druggability	Labels	Zoom	Positions
3				0.571
13				0.489
2				0.472

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK	Score	Probability
1	10.55	0.567
2	2.13	0.05
3	1.47	0.02

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

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, 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	2OOD	Q89NG0	151.1 Da LogP -0.77 TPSA 100.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)C(=O)NC(=N2)N`
TXC	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	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	Q9WTT6	—	150.1 Da LogP -0.48 TPSA 106.5	✓ Ro5	✓ Clean	`c1[nH]c2c(n1)c(nc(n2)N)N`
CHEMBL1224660	Q9WTT6	—	179.2 Da LogP -0.29 TPSA 77.7	✓ Ro5	✓ Clean	`CN(C)c1nc(=O)c2[nH]cnc2[nH]1`
CHEMBL321248	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	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	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	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	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	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	0.750	267.2 Da LogP -0.76 TPSA 125.1	✓ Ro5	✓ Clean	`CC(=O)OCCOCn1cnc2c(=O)[nH]c(N)nc21`
ZINC35900202	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	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	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	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	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	0.686	225.2 Da LogP -1.33 TPSA 119.0	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCCO)c(=O)[nH]1`
ZINC22052922	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	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	0.655	261.0 Da LogP 0.54 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(I)nc2[nH]cnc12`
ZINC4707072	0.655	214.0 Da LogP 0.70 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(Br)nc2[nH]cnc12`
ZINC6886310	0.655	261.0 Da LogP 0.54 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(I)c2nc[nH]c2n1`
ZINC2569523	0.643	305.2 Da LogP -1.21 TPSA 165.6	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCCOP(=O)(O)O)c(=O)[nH]1`
ZINC34036729	0.642	458.5 Da LogP 1.17 TPSA 163.4	✓ Ro5	✓ Clean	`CC(C)[C@H](NC(=O)OCc1ccccc1)C(=O)OCCOCn1cnc2c(=…`
ZINC4707332	0.625	214.2 Da LogP -1.42 TPSA 140.6	✓ Ro5	✓ Clean	`Nc1nc(S(N)(=O)=O)nc2[nH]cnc12`
ZINC6119301	0.596	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COC[C@H](O)CO)c(=O)[nH]1`
ZINC6119302	0.596	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COC[C@@H](O)CO)c(=O)[nH]1`
ZINC77293009	0.596	285.3 Da LogP -2.00 TPSA 148.5	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COCOC(CO)CO)c(=O)[nH]1`
ZINC13833539	0.595	208.2 Da LogP 0.21 TPSA 83.5	✓ Ro5	✓ Clean	`CCCCn1cnc2[nH]c(=O)[nH]c(=O)c21`
ZINC32496999	0.594	203.1 Da LogP 0.95 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(C(F)(F)F)c2nc[nH]c2n1`
ZINC5606355	0.594	203.1 Da LogP 0.95 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(C(F)(F)F)nc2[nH]cnc12`
ZINC1505	0.571	255.2 Da LogP -1.97 TPSA 139.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2COC(CO)CO)c(=O)[nH]1`
ZINC1800215	0.567	309.3 Da LogP -0.38 TPSA 128.2	✓ Ro5	✓ Clean	`CC(=O)Nc1nc2c(ncn2COCCOC(C)=O)c(=O)[nH]1`
ZINC1845515	0.566	207.2 Da LogP 0.36 TPSA 89.6	✓ Ro5	✓ Clean	`CC(C)Cn1cnc2c(=O)[nH]c(N)nc21`
ZINC1628375	0.559	211.2 Da LogP 1.60 TPSA 80.5	✓ Ro5	✓ Clean	`Nc1nc(-c2ccccc2)nc2[nH]cnc12`
ZINC1628378	0.559	226.2 Da LogP 1.18 TPSA 106.5	✓ Ro5	✓ Clean	`Nc1ccc(-c2nc(N)c3nc[nH]c3n2)cc1`
ZINC8616088	0.559	213.2 Da LogP -0.66 TPSA 114.6	✓ Ro5	✓ Clean	`CS(=O)(=O)c1nc(N)nc2[nH]cnc12`
ZINC22059880	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	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	0.545	209.2 Da LogP -0.65 TPSA 98.8	✓ Ro5	✓ Clean	`COCCn1cnc2c(=O)[nH]c(N)nc21`
ZINC1652244	0.545	221.3 Da LogP 0.75 TPSA 89.6	✓ Ro5	✓ Clean	`CC(C)CCn1cnc2c(=O)[nH]c(N)nc21`
ZINC8615379	0.543	209.3 Da LogP 1.44 TPSA 80.5	✓ Ro5	✓ Clean	`CC(C)Sc1nc(N)nc2[nH]cnc12`
ZINC91297460	0.543	204.2 Da LogP 0.54 TPSA 83.7	✓ Ro5	✓ Clean	`Nc1nc(N2CCCC2)c2nc[nH]c2n1`
ZINC81162221	0.537	209.2 Da LogP -1.21 TPSA 126.9	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2CC(=O)O)c(=O)[nH]1`
ZINC1682103	0.536	221.3 Da LogP 0.75 TPSA 89.6	✓ Ro5	✓ Clean	`CC[C@H](C)Cn1cnc2c(=O)[nH]c(N)nc21`
ZINC2044665	0.536	221.3 Da LogP 0.75 TPSA 89.6	✓ Ro5	✓ Clean	`CC[C@@H](C)Cn1cnc2c(=O)[nH]c(N)nc21`
ZINC2472815	0.533	267.2 Da LogP -0.96 TPSA 122.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nc2c(ncn2COCCO)c(=O)[nH]1`
ZINC33981136	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	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	0.528	226.2 Da LogP 1.68 TPSA 92.5	✓ Ro5	✓ Clean	`Nc1nc(Nc2ccccc2)c2nc[nH]c2n1`
ZINC3600430	0.527	239.2 Da LogP -1.70 TPSA 130.0	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2CC(CO)CO)c(=O)[nH]1`
ZINC1590047	0.526	212.2 Da LogP 1.00 TPSA 93.4	✓ Ro5	✓ Clean	`Nc1nc(-c2cccnc2)nc2[nH]cnc12`
ZINC1532183	0.517	289.2 Da LogP -1.15 TPSA 156.3	✓ Ro5	✓ Clean	`Nc1nc2c(ncn2CCOCP(=O)(O)O)c(=O)[nH]1`
ZINC13552969	0.514	219.3 Da LogP -0.66 TPSA 95.7	✓ Ro5	✓ Clean	`Nc1nc(N2CCNCC2)c2nc[nH]c2n1`
ZINC17298972	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.