Protein target profile

VK055_4003

urease, alpha subunit

Genome: KpATCC43816 Gene: AIK82550.1 ureC 3D evidence: Experimental + ColabFold model Metabolism 2 reactions UniProt A0A060VJP5

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Length 567

Pocket druggability 0.672

Metabolic reactions 2

Chokepoint No

Direct ligand evidence 0 59 total records

Functional annotation 1 EC 7 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

Experimental structure available At least one PDB experimental structure is loaded, not just a predicted model - stronger structural coverage than AlphaFold/ColabFold alone. Central metabolic position More central than 90.4% of genes in this genome. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. Second pocket predictor agrees P2Rank predicted binding-site probability 0.62. 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: No hit
Gut microbiome similarity: 7.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 62.61 Higher values support similarity to known essential genes.
DEG E-value: 0.0 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 98.16 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

PDB experimental structure

The selected pocket score is the FPocket value used for ranking after applying the curated structure priority. It estimates small-molecule pocket quality; it is not experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

FPocket 0.672

Structure 8HCN

Pocket Pocket 5

P2Rank 0.619

Structure 8HCN

Pocket Pocket 1

ColabFold model

FPocket 0.687 · Pocket 1

P2Rank 0.117 · Pocket 1

Core conservation Accessory gene

Roary accessory

CoreCruncher accessory

Gut microbiome 352 / 4744 genomes with a hit

Prevalence 7.4%

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Metabolic context

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

Explore metabolic network

Metabolic context: more central than 90.4% of genes in this genome, no human homolog detected.

Relative network centrality 90.4% more central than 90.4% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDVQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCHHLDPDIAEDVAFAESRIRRETIAAEDVLHDLGAFSLTSSDSQAMGRVGEVILRTWQVAHRMKVQRGALAEETGDNDNFRVKRYIAKYTINPALTHGIAHEVGSIEVGKLADLVVWSPAFFGVKPATVIKGGMIAIAPMGDINASIPTPQPVHYRPMFGALGSARHHCRLTFLSQAAAANGVAERLNLRSAIAVVKGCRTVQKADMVHNSLQPNITVDAQTYEVRVDGELITSEPADVLPMAQRYFLF

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 domains and features

Domain and signature matches imported from InterPro and related databases.

34 records

Show feature table

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

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 · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #5

0.672

Unusual size

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Surrounding area

Site 2 FPocket #10

0.601

Likely same site as P2Rank 2 1.7 Å 9 shared residues 100% of smaller site

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Surrounding area

Site 3 FPocket #2

0.454

Likely same site as P2Rank 1 3.5 Å 15 shared residues 75% of smaller site

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Surrounding area

Site 4 FPocket #20

0.313

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.619

Likely same site as FPocket 2 3.5 Å 15 shared residues 75% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.085

Likely same site as FPocket 10 1.7 Å 9 shared residues 100% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.034

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Surrounding area

Site 4 P2Rank #4

0.028

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Surrounding area

Binding pockets · FPocket

Druggability: high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Site 1 FPocket #1

0.687

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Surrounding area

Site 2 FPocket #14

0.34

Unusual size

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Surrounding area

Site 3 FPocket #10

0.335

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Surrounding area

Site 4 FPocket #9

0.322

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Surrounding area

Binding pockets · P2Rank

Probability: high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Site 1 P2Rank #1

0.117

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Surrounding area

Site 2 P2Rank #2

0.078

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Surrounding area

Site 3 P2Rank #3

0.061

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Surrounding area

Site 4 P2Rank #4

0.05

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Surrounding area

Site 5 P2Rank #5

0.016

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Surrounding area

Residue sets

UniProt: Active site:320-320 Proton donor

UniProt: Binding site:134-134

UniProt: Binding site:136-136

UniProt: Binding site:217-217 via carbamate group

UniProt: Binding site:219-219

UniProt: Binding site:246-246

UniProt: Binding site:272-272

UniProt: Binding site:360-360

All structural evidence 1 experimental · 1 predicted

Structural evidence

1 + 1

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
PDB 8HCN	X-ray	—	C	—	PDBe RCSB PDBj File	Viewing
ColabFold VK055_4003	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.

59 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 9 records from similar proteins

Structural ligands 9 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

2PA PDB via homolog 96.0 Da · LogP -1.00 · TPSA 89.3 Open detail RCSB PDB

9XN PDB via homolog Detail RCSB PDB

BO3 PDB via homolog Detail RCSB PDB

CO2 PDB via homolog Detail RCSB PDB

DBX 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
2PA RCSB PDB	3UBP	P41020	96.0 Da LogP -1.00 TPSA 89.3	✓ Ro5	✓ Clean	`NP(=O)(N)O`
9XN RCSB PDB	5OL4	P41020	113.1 Da LogP -0.85 TPSA 66.5	✓ Ro5	✓ Clean	`NP(=S)(O)O`
BO3 RCSB PDB	1S3T	P41020	61.8 Da LogP -2.05 TPSA 60.7	✓ Ro5	✓ Clean	`B(O)(O)O`
CO2 RCSB PDB	1KRC	P18314	44.0 Da LogP -0.58 TPSA 34.1	✓ Ro5	✓ Clean	`C(=O)=O`
DBX RCSB PDB	5FSD	P41020	190.2 Da LogP 0.34 TPSA 94.8	✓ Ro5	✓ Clean	`c1cc(c(cc1O)S(=O)(=O)O)O`
DJM RCSB PDB	6ZJA	P69996	277.3 Da LogP 2.09 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(cc(c1)n2ccnc2SCC(=O)NO)C`
FLC RCSB PDB	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 RCSB PDB	1FWE	P18314	75.1 Da LogP -0.49 TPSA 49.3	✓ Ro5	✓ Clean	`CC(=O)NO`
HQE RCSB PDB	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 ZINC	1.000	277.3 Da LogP 2.09 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NO)c1`
ZINC7056601 ZINC	0.805	275.4 Da LogP 2.33 TPSA 46.9	✓ Ro5	✓ Clean	`CNC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC2468176 ZINC	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 ZINC	0.750	291.4 Da LogP 2.26 TPSA 56.1	✓ Ro5	✓ Clean	`CONC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC7283167 ZINC	0.733	301.4 Da LogP 2.86 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CC2)c1`
ZINC169299564 ZINC	0.732	262.3 Da LogP 2.67 TPSA 55.1	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)O)c1`
ZINC13558894 ZINC	0.727	262.3 Da LogP 4.43 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(-c2ccc(-c3ccc(O)cc3)cc2)cc1`
ZINC2723090 ZINC	0.717	351.5 Da LogP 4.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC427372 ZINC	0.717	329.5 Da LogP 3.64 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CCCC2)c1`
ZINC2468174 ZINC	0.708	416.3 Da LogP 4.98 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(Br)cc2)c1`
ZINC427368 ZINC	0.702	337.4 Da LogP 4.22 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccccc2)c1`
ZINC427369 ZINC	0.702	343.5 Da LogP 4.03 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CCCCC2)c1`
ZINC7056925 ZINC	0.702	333.4 Da LogP 1.87 TPSA 73.2	✓ Ro5	✓ Clean	`COC(=O)CNC(=O)CSc1nccn1-c1cc(C)cc(C)c1`
ZINC18335421 ZINC	0.688	353.4 Da LogP 3.93 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(O)cc2)c1`
ZINC2468188 ZINC	0.688	342.4 Da LogP 3.52 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cc(C)on2)c1`
ZINC4249532 ZINC	0.674	249.3 Da LogP 1.47 TPSA 67.2	✓ Ro5	✓ Clean	`O=C(CSc1nccn1-c1ccccc1)NO`
ZINC2468165 ZINC	0.673	359.5 Da LogP 3.38 TPSA 72.7	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2nnc(C)s2)c1`
ZINC2723088 ZINC	0.673	355.4 Da LogP 4.36 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(F)cc2)c1`
ZINC2723091 ZINC	0.673	351.5 Da LogP 4.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)c1`
ZINC2723094 ZINC	0.673	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cc(C)ccc2C)c1`
ZINC2723095 ZINC	0.673	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(C)cc2C)c1`
ZINC2723100 ZINC	0.673	371.9 Da LogP 4.87 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(Cl)cc2)c1`
ZINC427370 ZINC	0.673	344.5 Da LogP 3.68 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2nccs2)c1`
ZINC10271325 ZINC	0.660	342.4 Da LogP 3.52 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cc(C)no2)c1`
ZINC10271326 ZINC	0.660	328.4 Da LogP 3.21 TPSA 73.0	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccon2)c1`
ZINC12547709 ZINC	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 ZINC	0.660	365.5 Da LogP 4.78 TPSA 46.9	✓ Ro5	✓ Clean	`CCc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC456077698 ZINC	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 ZINC	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 ZINC	0.660	345.5 Da LogP 2.88 TPSA 56.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NC2CCOCC2)c1`
ZINC1700194 ZINC	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 ZINC	0.652	283.7 Da LogP 2.12 TPSA 67.2	✓ Ro5	✓ Clean	`O=C(CSc1nccn1-c1cccc(Cl)c1)NO`
ZINC11544611 ZINC	0.647	352.5 Da LogP 3.29 TPSA 59.8	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)NCc2ccccn2)c1`
ZINC2723087 ZINC	0.647	367.5 Da LogP 4.23 TPSA 56.1	✓ Ro5	✓ Clean	`COc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC2723089 ZINC	0.647	355.4 Da LogP 4.36 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccccc2F)c1`
ZINC2723093 ZINC	0.647	365.5 Da LogP 4.84 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(C)c2C)c1`
ZINC2723101 ZINC	0.647	371.9 Da LogP 4.87 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(Cl)c2)c1`
ZINC54659994 ZINC	0.647	343.4 Da LogP 2.91 TPSA 85.8	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2nc(C)no2)c1`
ZINC7120438 ZINC	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 ZINC	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 ZINC	0.647	353.4 Da LogP 3.93 TPSA 67.2	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(O)c2)c1`
ZINC11544195 ZINC	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 ZINC	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 ZINC	0.640	351.5 Da LogP 4.53 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(NC(=O)CSc2nccn2-c2cccc(C)c2)c1`
ZINC58947296 ZINC	0.638	315.4 Da LogP 3.20 TPSA 38.1	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)N2CCCC2)c1`
ZINC2468183 ZINC	0.635	373.4 Da LogP 4.50 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2ccc(F)cc2F)c1`
ZINC2723092 ZINC	0.635	381.5 Da LogP 4.62 TPSA 56.1	✓ Ro5	✓ Clean	`CCOc1ccc(NC(=O)CSc2nccn2-c2cc(C)cc(C)c2)cc1`
ZINC2723102 ZINC	0.635	355.4 Da LogP 4.36 TPSA 46.9	✓ Ro5	✓ Clean	`Cc1cc(C)cc(-n2ccnc2SCC(=O)Nc2cccc(F)c2)c1`
ZINC7120429 ZINC	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 ZINC	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.

VK055_4003

Promising target candidate with multiple supporting evidence streams.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Structure

Pathways

Metabolic context

Sequence

Functional annotations

Enzyme Commission (EC)

Gene Ontology (GO)

Sequence domains and features

3D structure

Binding pockets · FPocket

Binding pockets · P2Rank

Binding pockets · FPocket

Binding pockets · P2Rank

Structural evidence

Ligand evidence