Protein profile

VK055_4194

urease, alpha subunit

Genome: KpATCC43816

Gene: ureC2 AIK82739.1 Structure source: AlphaFold + ColabFold UniProt A0A2L1BU89

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Amino acids 572

Annotations 8

Features 34

PDB binders 9

Druggability 0.831

Overview

Basic information about this protein and its source genome.

Accession: VK055_4194
Assembly: Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene: ureC2 AIK82739.1
Status: annotated
Amino acids: 572
Structure source: AlphaFold + ColabFold

3.5.1.5

GO:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds. GO:0009039 Catalysis of the reaction: urea + 2 H2O + H+ = hydrogencarbonate + 2 NH4+. GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. GO:0016151 Binding to a nickel (Ni) cation. 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 (%): 55.185
DEG E-value: 0.0
Localization: Cytoplasmic
ColabFold pLDDT: 97.8

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 0.831

Structure A0A2L1BU89

Pocket Pocket 20

P2Rank 0.146

Structure A0A2L1BU89

Pocket Pocket 1

ColabFold model

FPocket 0.932 · Pocket 7

P2Rank 0.18 · 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:0016810 Catalysis of the hydrolysis of any carbon-nitrogen bond, C-N, with the exception of peptide bonds.
GO:0009039 Catalysis of the reaction: urea + 2 H2O + H+ = hydrogencarbonate + 2 NH4+.
GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
GO:0016151 Binding to a nickel (Ni) cation.
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
132	145	ProSitePatterns	PS01120	Urease nickel ligands signature.
132	145	InterPro	IPR029754	Urease nickel binding site
130	459	Pfam	PF01979	Amidohydrolase family
130	459	InterPro	IPR006680	Amidohydrolase-related
2	572	Hamap	MF_01953	Urease subunit alpha [ureC].
2	572	InterPro	IPR005848	Urease, alpha subunit
414	484	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
414	484	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
134	572	ProSiteProfiles	PS51368	Urease domain profile.
134	572	InterPro	IPR017951	Urease alpha subunit, C-terminal
4	571	NCBIfam	TIGR01792	urease subunit alpha
4	571	InterPro	IPR005848	Urease, alpha subunit
134	570	Gene3D	G3DSA:3.20.20.140	-
322	338	ProSitePatterns	PS00145	Urease active site.
322	338	InterPro	IPR017950	Urease active site
3	571	PANTHER	PTHR43440	UREASE
2	182	SUPERFAMILY	SSF51338	Composite domain of metallo-dependent hydrolases
2	182	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
135	571	SUPERFAMILY	SSF51556	Metallo-dependent hydrolases
135	571	InterPro	IPR032466	Metal-dependent hydrolase
3	124	Pfam	PF00449	Urease alpha-subunit, N-terminal domain
3	124	InterPro	IPR011612	Urease alpha-subunit, N-terminal domain
432	445	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
432	445	InterPro	IPR005848	Urease, alpha subunit
406	421	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
406	421	InterPro	IPR005848	Urease, alpha subunit
339	355	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
339	355	InterPro	IPR005848	Urease, alpha subunit
300	317	PRINTS	PR01752	Urea amidohydrolase (urease) protein signature
300	317	InterPro	IPR005848	Urease, alpha subunit
4	485	Gene3D	G3DSA:2.30.40.10	Urease, subunit C, domain 1
4	485	InterPro	IPR011059	Metal-dependent hydrolase, composite domain superfamily
3	570	CDD	cd00375	Urease_alpha
3	570	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

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_A0A2L1BU89	AlphaFold	—	—	full sequence	—	Viewing
ColabFold VK055_4194	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
20				0.831
16				0.473
30				0.25

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	3.54	0.13
2	2.09	0.047
3	1.2	0.011

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
7				0.932
5				0.64
1				0.217

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	Sticks	Spheres	Surfaces	Score	Probability	Labels	Zoom	Positions
1				2.16	0.051
2				1.33	0.015

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	4H9M	P07374	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.