Protein profile

KP13_02816

Urease subunit alpha

Genome: KpKP13

Gene: AHE42614.1 ureC Structure source: Experimental + ColabFold UniProt A0A060VJP5

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Amino acids 624

Annotations 8

Features 34

PDB binders 9

Druggability 0.672

Overview

Basic information about this protein and its source genome.

Accession: KP13_02816
Assembly: Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene: AHE42614.1 ureC
Status: annotated
Amino acids: 624
Structure source: Experimental + ColabFold

3.5.1.5

GO:0016151 Binding to a nickel (Ni) cation. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0009039 Catalysis of the reaction: urea + 2 H2O + H+ = hydrogencarbonate + 2 NH4+. GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds. GO:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen. GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

Target profile

Computed evidence for target prioritization.

Human off-target: No hit
Human identity (%): 0.0
Gut microbiome off-target: hit
Essential (DEG): Y
DEG identity (%): 62.191
DEG E-value: 0.0
Localization: CytoplasmicMembrane
ColabFold pLDDT: 93.33

Selected Druggability evidence

PDB experimental structure

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 0.672

Structure 8HCN

Pocket Pocket 5

P2Rank 0.619

Structure 8HCN

Pocket Pocket 1

ColabFold model

FPocket 0.421 · Pocket 19

P2Rank 0.087 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 352 / 4744 genomes with a hit

Normalized 0.074

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

3.5.1.5

Gene Ontology (GO)

GO:0016151 Binding to a nickel (Ni) cation.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0009039 Catalysis of the reaction: urea + 2 H2O + H+ = hydrogencarbonate + 2 NH4+.
GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
GO:0006807 OBSOLETE. The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0043419 The chemical reactions and pathways resulting in the breakdown of urea, the water soluble compound O=C-(NH2)2.

Sequence Features

Domain/signature hits from InterPro and related databases.

34 records

Show feature table

Start	End	DB	Term	Name
3	119	Pfam	PF00449	Urease alpha-subunit, N-terminal domain
3	119	InterPro	IPR011612	Urease alpha-subunit, N-terminal domain
125	453	Pfam	PF01979	Amidohydrolase family
125	453	InterPro	IPR006680	Amidohydrolase-related
127	140	ProSitePatterns	PS01120	Urease nickel ligands signature.
127	140	InterPro	IPR029754	Urease nickel binding site
3	566	CDD	cd00375	Urease_alpha
3	566	InterPro	IPR005848	Urease, alpha subunit
295	312	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
295	312	InterPro	IPR005848	Urease, alpha subunit
427	440	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
427	440	InterPro	IPR005848	Urease, alpha subunit
334	350	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
334	350	InterPro	IPR005848	Urease, alpha subunit
401	416	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
401	416	InterPro	IPR005848	Urease, alpha subunit
317	333	ProSitePatterns	PS00145	Urease active site.
317	333	InterPro	IPR017950	Urease active site
2	567	Hamap	MF_01953	Urease subunit alpha [ureC].
2	567	InterPro	IPR005848	Urease, alpha subunit
129	567	ProSiteProfiles	PS51368	Urease domain profile.
129	567	InterPro	IPR017951	Urease alpha subunit, C-terminal
130	566	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
130	566	InterPro	IPR032466	Metal-dependent hydrolase
2	177	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
2	177	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
422	477	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
422	477	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
129	562	Gene3D	G3DSA:3.20.20.140	-
4	480	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
4	480	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
3	566	PANTHER	PTHR43440	UREASE
4	566	NCBIfam	TIGR01792	urease subunit alpha
4	566	InterPro	IPR005848	Urease, alpha subunit

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

1 + 1

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

Entry	Method	Resolution	Chain	Coverage	Links	Status
PDB 8HCN	X-ray	20.00 Å	-	—	PDBe RCSB PDBj File	Viewing
ColabFold KP13_02816	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
45				0.924
3				0.821
47				0.8
7				0.672

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	21.0	0.864
2	16.33	0.776
3	14.14	0.713
4	13.01	0.671
5	12.75	0.661

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
19				0.421
16				0.411
9				0.397
2				0.3

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	2.75	0.083
2	1.4	0.017
3	1.22	0.011
4	0.97	0.005

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.

59 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
2PA	3UBP	P41020	96.0 Da LogP -1.00 TPSA 89.3	✓ Ro5	✓ Clean	`NP(=O)(N)O`
9XN	5OL4	P41020	113.1 Da LogP -0.85 TPSA 66.5	✓ Ro5	✓ Clean	`NP(=S)(O)O`
BO3	1S3T	P41020	61.8 Da LogP -2.05 TPSA 60.7	✓ Ro5	✓ Clean	`B(O)(O)O`
CO2	1KRC	P18314	44.0 Da LogP -0.58 TPSA 34.1	✓ Ro5	✓ Clean	`C(=O)=O`
DBX	5FSD	P41020	190.2 Da LogP 0.34 TPSA 94.8	✓ Ro5	✓ Clean	`c1cc(c(cc1O)S(=O)(=O)O)O`
DJM	6ZJA	P69996	277.3 Da LogP 2.09 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(cc(c1)n2ccnc2SCC(=O)NO)C`
FLC	4AC7	P41020	189.1 Da LogP -5.25 TPSA 140.6	✓ Ro5	✓ Clean	`C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O`
HAE	1FWE	P18314	75.1 Da LogP -0.49 TPSA 49.3	✓ Ro5	✓ Clean	`CC(=O)NO`
HQE	5FSE	P41020	110.1 Da LogP 1.10 TPSA 40.5	✓ Ro5	✓ Clean	`c1cc(ccc1O)O`

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
ZINC11613699	1.000	277.3 Da LogP 2.09 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NO)c1`
ZINC7056601	0.805	275.4 Da LogP 2.33 TPSA 46.9	✓ Ro5	✓ Clean	`CNC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC2468176	0.767	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)c1`
ZINC11252349	0.750	291.4 Da LogP 2.26 TPSA 56.1	✓ Ro5	✓ Clean	`CONC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC7283167	0.733	301.4 Da LogP 2.86 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CC2)c1`
ZINC169299564	0.732	262.3 Da LogP 2.67 TPSA 55.1	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)O)c1`
ZINC13558894	0.727	262.3 Da LogP 4.43 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(-c2ccc(-c3ccc(O)cc3)cc2)cc1`
ZINC2723090	0.717	351.5 Da LogP 4.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC427372	0.717	329.5 Da LogP 3.64 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CCCC2)c1`
ZINC2468174	0.708	416.3 Da LogP 4.98 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(Br)cc2)c1`
ZINC427368	0.702	337.4 Da LogP 4.22 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccccc2)c1`
ZINC427369	0.702	343.5 Da LogP 4.03 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CCCCC2)c1`
ZINC7056925	0.702	333.4 Da LogP 1.87 TPSA 73.2	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC18335421	0.688	353.4 Da LogP 3.93 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(O)cc2)c1`
ZINC2468188	0.688	342.4 Da LogP 3.52 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cc(C)on2)c1`
ZINC4249532	0.674	249.3 Da LogP 1.47 TPSA 67.2	✓ Ro5	✓ Clean	`O=C(CSc1nccn1-c1ccccc1)NO`
ZINC2468165	0.673	359.5 Da LogP 3.38 TPSA 72.7	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2nnc(C)s2)c1`
ZINC2723088	0.673	355.4 Da LogP 4.36 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(F)cc2)c1`
ZINC2723091	0.673	351.5 Da LogP 4.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)c1`
ZINC2723094	0.673	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cc(C)ccc2C)c1`
ZINC2723095	0.673	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(C)cc2C)c1`
ZINC2723100	0.673	371.9 Da LogP 4.87 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(Cl)cc2)c1`
ZINC427370	0.673	344.5 Da LogP 3.68 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2nccs2)c1`
ZINC10271325	0.660	342.4 Da LogP 3.52 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cc(C)no2)c1`
ZINC10271326	0.660	328.4 Da LogP 3.21 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccon2)c1`
ZINC12547709	0.660	369.5 Da LogP 3.57 TPSA 64.7	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2c(C)nn(C)c2C)c1`
ZINC2723103	0.660	365.5 Da LogP 4.78 TPSA 46.9	✓ Ro5	✓ Clean	`CCc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC456077698	0.660	361.5 Da LogP 3.25 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)N[C@@H](C)CC(C)(C)O)c1`
ZINC456077702	0.660	361.5 Da LogP 3.25 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)N[C@H](C)CC(C)(C)O)c1`
ZINC84086012	0.660	345.5 Da LogP 2.88 TPSA 56.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CCOCC2)c1`
ZINC1700194	0.654	254.2 Da LogP -0.11 TPSA 129.0	✓ Ro5	✓ Clean	`O=S(=O)(O)c1ccc(O)c(S(=O)(=O)O)c1`
ZINC4249534	0.652	283.7 Da LogP 2.12 TPSA 67.2	✓ Ro5	✓ Clean	`O=C(CSc1nccn1-c1cccc(Cl)c1)NO`
ZINC11544611	0.647	352.5 Da LogP 3.29 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NCc2ccccn2)c1`
ZINC2723087	0.647	367.5 Da LogP 4.23 TPSA 56.1	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC2723089	0.647	355.4 Da LogP 4.36 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccccc2F)c1`
ZINC2723093	0.647	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(C)c2C)c1`
ZINC2723101	0.647	371.9 Da LogP 4.87 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(Cl)c2)c1`
ZINC54659994	0.647	343.4 Da LogP 2.91 TPSA 85.8	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2nc(C)no2)c1`
ZINC7120438	0.647	360.5 Da LogP 2.22 TPSA 76.0	✓ Ro5	✓ Clean	`CCNC(=O)[C@@H](C)NC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC7120440	0.647	360.5 Da LogP 2.22 TPSA 76.0	✓ Ro5	✓ Clean	`CCNC(=O)[C@H](C)NC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC98073415	0.647	353.4 Da LogP 3.93 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(O)c2)c1`
ZINC11544195	0.642	408.6 Da LogP 4.00 TPSA 50.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC[C@@H](c2ccccc2)N(C…`
ZINC11544198	0.642	408.6 Da LogP 4.00 TPSA 50.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC[C@H](c2ccccc2)N(C)…`
ZINC2723023	0.640	351.5 Da LogP 4.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(NC(=O)CSc2nccn2-c2cccc(C)c2)c1`
ZINC58947296	0.638	315.4 Da LogP 3.20 TPSA 38.1	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)N2CCCC2)c1`
ZINC2468183	0.635	373.4 Da LogP 4.50 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(F)cc2F)c1`
ZINC2723092	0.635	381.5 Da LogP 4.62 TPSA 56.1	✓ Ro5	✓ Clean	`CCOc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC2723102	0.635	355.4 Da LogP 4.36 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(F)c2)c1`
ZINC7120429	0.635	374.5 Da LogP 2.61 TPSA 76.0	✓ Ro5	✓ Clean	`CCCNC(=O)[C@@H](C)NC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC7120432	0.635	374.5 Da LogP 2.61 TPSA 76.0	✓ Ro5	✓ Clean	`CCCNC(=O)[C@H](C)NC(=O)CSc1nccn1-c1cc(C)cc(C)c1`

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.