Protein target profile

VK055_2800

ornithine carbamoyltransferase

Genome: KpATCC43816 Gene: AIK81389.1 argF 3D evidence: Experimental + ColabFold model Metabolism 1 reaction UniProt A0A0H3GHJ1

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Length 334

Pocket druggability 0.453

Metabolic reactions 1

Chokepoint No

Direct ligand evidence 0 65 total records

Functional annotation 1 EC 8 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 94.2% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. 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 (%): 36.89 Lower values reduce human off-target concern.
Human E-value: 2.9500000000000004e-56
Gut microbiome similarity: 42.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 38.298 Higher values support similarity to known essential genes.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.21 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 0.453

Structure 7TMD

Pocket Pocket 1

P2Rank 0.436

Structure 7TMD

Pocket Pocket 1

ColabFold model

FPocket 0.922 · Pocket 1

P2Rank 0.699 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 1998 / 4744 genomes with a hit

Prevalence 42.1%

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 94.2% of genes in this genome.

Relative network centrality 94.2% more central than 94.2% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSAFYQKHFLKLLDFTPAEITALLELAAKLKADKKNGIEVQKLAGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGHGQEVVETLAQYAGVPVWNGLTNEFHPTQLLADLLTMKEHLPGKAFNQMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPSACWPEAALVETCTALAKQQGGNITLTEDIAAGVKGADFIYTDVWVSMGEAKEKWAERIALLRDYQVNSAMLALTGNPQVKFLHCLPAFHDDQTTLGKQMAADYGLHGGMEVTDEVFESAASVVFDQAENRMHTIKAVMVATLSR

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

2.1.3.3

Gene Ontology (GO)

GO:0016743 Catalysis of the transfer of a carboxyl- or carbamoyl group from one compound (donor) to another (acceptor).
GO:0006591 The chemical reactions and pathways involving ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.
GO:0016597 Binding to an amino acid, organic acids containing one or more amino substituents.
GO:0004585 Catalysis of the reaction: carbamoyl phosphate + L-ornithine = phosphate + L-citrulline.
GO:0006520 The chemical reactions and pathways involving amino acids, carboxylic acids containing one or more amino groups.
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
GO:0019240 The chemical reactions and pathways resulting in the formation of citrulline, N5-carbamoyl-L-ornithine, an alpha amino acid not found in proteins.
GO:0042450 OBSOLETE. The chemical reactions and pathways resulting in the formation of arginine (2-amino-5-guanidinopentanoic acid) via the intermediate compound ornithine.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

36 records

Show feature table

Start	End	DB	Term	Name
6	332	Gene3D	G3DSA:3.40.50.1370	Aspartate/ornithine carbamoyltransferase
6	332	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
229	239	PRINTS	PR00102	Ornithine carbamoyltransferase signature
229	239	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
83	96	PRINTS	PR00102	Ornithine carbamoyltransferase signature
83	96	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
123	137	PRINTS	PR00102	Ornithine carbamoyltransferase signature
123	137	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
50	64	PRINTS	PR00102	Ornithine carbamoyltransferase signature
50	64	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
311	322	PRINTS	PR00102	Ornithine carbamoyltransferase signature
311	322	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
152	319	FunFam	G3DSA:3.40.50.1370:FF:000004	Ornithine carbamoyltransferase
52	71	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
52	71	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
134	145	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
134	145	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
297	320	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
297	320	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
267	276	PRINTS	PR00100	Aspartate/ornithine carbamoyltransferase superfamily signature
267	276	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
7	147	Pfam	PF02729	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain
7	147	InterPro	IPR006132	Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding
156	330	Pfam	PF00185	Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain
156	330	InterPro	IPR006131	Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain
152	319	Gene3D	G3DSA:3.40.50.1370	Aspartate/ornithine carbamoyltransferase
152	319	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
7	332	NCBIfam	TIGR00658	ornithine carbamoyltransferase
7	332	InterPro	IPR002292	Ornithine/putrescine carbamoyltransferase
2	333	SUPERFAMILY	SSF53671	Aspartate/ornithine carbamoyltransferase
2	333	InterPro	IPR036901	Aspartate/ornithine carbamoyltransferase superfamily
6	333	Hamap	MF_01109	Ornithine carbamoyltransferase, catabolic [argI].
6	333	InterPro	IPR024904	Ornithine carbamoyltransferase
52	59	ProSitePatterns	PS00097	Aspartate and ornithine carbamoyltransferases signature.
52	59	InterPro	IPR006130	Aspartate/ornithine carbamoyltransferase
3	333	PANTHER	PTHR45753	ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL

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 #1

0.453

Show in viewer

Surrounding area

Site 2 FPocket #2

0.45

Unusual size

Show in viewer

Surrounding area

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.436

Show in viewer

Surrounding area

Site 2 P2Rank #2

0.005

Show in viewer

Surrounding area

Residue sets

UniProt: Binding site:107-107

UniProt: Binding site:134-137

UniProt: Binding site:168-168

UniProt: Binding site:232-232

UniProt: Binding site:236-237

UniProt: Binding site:274-275

UniProt: Binding site:320-320

UniProt: Binding site:56-59

UniProt: Binding site:83-83

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 7TMD	X-ray	2.35 Å	A,B,C,D,E,F	100.0% 1-334	PDBe RCSB PDBj File	Viewing
ColabFold VK055_2800	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.

65 records

Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records

Transferred evidence 15 records from similar proteins

Structural ligands 15 0 loaded crystals

Measured bioactivity 0 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

1NP PDB via homolog 144.2 Da · LogP 2.55 · TPSA 20.2 Open detail RCSB PDB

8H8 PDB via homolog Detail RCSB PDB

98T PDB via homolog Detail RCSB PDB

CIR PDB via homolog Detail RCSB PDB

CP 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
1NP RCSB PDB	7NNY	P9WIT9	144.2 Da LogP 2.55 TPSA 20.2	✓ Ro5	✓ Clean	`c1ccc2c(c1)cccc2O`
8H8 RCSB PDB	7NOR	P9WIT9	137.1 Da LogP 1.40 TPSA 44.0	✓ Ro5	✓ Clean	`c1cc(c(cc1O)F)C#N`
98T RCSB PDB	7NNW	P9WIT9	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(c(c1)I)O`
CIR RCSB PDB	4JQO	Q8DCF5	175.2 Da LogP -1.15 TPSA 118.4	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CNC(=O)N`
CP RCSB PDB	4H31	Q8DCF5	141.0 Da LogP -0.83 TPSA 109.9	✓ Ro5	✓ Clean	`C(=O)(N)OP(=O)(O)O`
NMR RCSB PDB	7NOU	P9WIT9	—	—	—	`B(=O)(c1cc(cc(c1)Cl)Cl)O`
NVA RCSB PDB	4NF2	Q81M99	117.1 Da LogP 0.20 TPSA 63.3	✓ Ro5	✓ Clean	`CCC[C@@H](C(=O)O)N`
PAO RCSB PDB	2OTC	P04391	254.2 Da LogP -1.53 TPSA 149.9	✓ Ro5	✓ Clean	`C(C[C@@H](C(=O)O)N)CNC(=O)CP(=O)(O)O`
PE5 RCSB PDB	4H31	Q8DCF5	398.5 Da LogP 0.13 TPSA 94.1	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCOCCO`
PSQ RCSB PDB	1DUV	P04391	290.2 Da LogP -1.77 TPSA 184.8	1 viol.	✓ Clean	`C(C[C@@H](C(=O)O)N)CN[P@](=O)(N)NS(=O)(=O)O`
PTZ RCSB PDB	7NNZ	P9WIT9	190.3 Da LogP 2.70 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1c(nc(s1)N)c2ccccc2`
PUW RCSB PDB	4A8H	Q837U7	210.2 Da LogP -0.98 TPSA 112.7	✓ Ro5	✓ Clean	`C(CCNC(=O)CP(=O)(O)O)CN`
UJZ RCSB PDB	7NOS	P9WIT9	265.0 Da LogP 3.34 TPSA 28.7	✓ Ro5	✓ Clean	`c1c(cc(c2c1[nH]cn2)Br)C(F)(F)F`
UK2 RCSB PDB	7NOV	P9WIT9	181.0 Da LogP -0.42 TPSA 83.6	✓ Ro5	✓ Clean	`B(c1ccc(c(c1)[N+](=O)[O-])C)(O)O`
UKH RCSB PDB	7NP0	P9WIT9	166.9 Da LogP -0.73 TPSA 83.6	✓ Ro5	✓ Clean	`B(c1ccc(cc1)[N+](=O)[O-])(O)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
ZINC2548331 ZINC	1.000	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(O)c(I)c1`
ZINC5650743 ZINC	1.000	222.3 Da LogP 0.07 TPSA 57.2	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCO`
ZINC6403917 ZINC	1.000	354.4 Da LogP 0.11 TPSA 84.8	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCCOCCO`
ZINC20340495 ZINC	0.926	266.4 Da LogP 4.37 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1ccc(-c2ccccc2)cc1`
ZINC84123 ZINC	0.750	204.3 Da LogP 3.01 TPSA 38.9	✓ Ro5	Alert	`Cc1ccc(-c2nc(N)sc2C)cc1`
ZINC8700304 ZINC	0.733	278.0 Da LogP 1.78 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(I)c(O)c1`
ZINC258828063 ZINC	0.719	204.1 Da LogP 2.72 TPSA 28.7	✓ Ro5	✓ Clean	`Fc1cc(C(F)(F)F)cc2[nH]cnc12`
ZINC2032126 ZINC	0.714	244.3 Da LogP 4.85 TPSA 20.2	✓ Ro5	✓ Clean	`Oc1cccc2c1ccc1c3ccccc3ccc21`
ZINC12501520 ZINC	0.688	458.5 Da LogP -0.88 TPSA 123.5	1 viol.	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC3874716 ZINC	0.688	414.5 Da LogP -0.90 TPSA 114.3	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC41656314 ZINC	0.688	204.3 Da LogP 3.01 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1cccc(-c2nc(N)sc2C)c1`
ZINC4283769 ZINC	0.688	238.3 Da LogP -0.96 TPSA 77.4	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCO`
ZINC4521548 ZINC	0.688	282.3 Da LogP -0.95 TPSA 86.6	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCO`
ZINC5178829 ZINC	0.688	326.4 Da LogP -0.93 TPSA 95.8	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCO`
ZINC5178830 ZINC	0.688	370.4 Da LogP -0.91 TPSA 105.1	✓ Ro5	✓ Clean	`OCCOCCOCCOCCOCCOCCOCCOCCO`
ZINC5859031 ZINC	0.688	294.4 Da LogP 1.13 TPSA 55.4	✓ Ro5	✓ Clean	`CCOCCOCCOCCOCCOCCOCC`
ZINC1009200 ZINC	0.677	208.3 Da LogP 2.84 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1ccc(F)cc1`
ZINC115331 ZINC	0.677	269.2 Da LogP 3.46 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1ccc(Br)cc1`
ZINC2528189 ZINC	0.677	320.1 Da LogP 1.86 TPSA 52.6	✓ Ro5	✓ Clean	`COC(=O)c1ccc(C(=O)OC)c(I)c1`
ZINC2559798 ZINC	0.677	276.1 Da LogP 2.39 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(C)c(I)c1`
ZINC28014904 ZINC	0.677	206.3 Da LogP 2.41 TPSA 59.1	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1ccc(O)cc1`
ZINC7580 ZINC	0.677	224.7 Da LogP 3.35 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1ccc(Cl)cc1`
ZINC1570993 ZINC	0.667	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@H](N)C(=O)O`
ZINC1570999 ZINC	0.667	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCC[C@H](N)C(=O)O`
ZINC1620974 ZINC	0.667	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@H](N)C(=O)O`
ZINC1742220 ZINC	0.667	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCC[C@H](N)C(=O)O`
ZINC2035155 ZINC	0.667	215.3 Da LogP 2.93 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCC[C@@H](N)C(=O)O`
ZINC2035157 ZINC	0.667	201.3 Da LogP 2.54 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCC[C@@H](N)C(=O)O`
ZINC2037129 ZINC	0.667	243.4 Da LogP 3.71 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCC[C@@H](N)C(=O)O`
ZINC39951743 ZINC	0.667	292.1 Da LogP 2.17 TPSA 46.5	✓ Ro5	✓ Clean	`CCOC(=O)c1ccc(O)c(I)c1`
ZINC43531622 ZINC	0.667	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[C@H](N)C(=O)O`
ZINC43531626 ZINC	0.667	271.4 Da LogP 4.49 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCCCCC[C@@H](N)C(=O)O`
ZINC8437446 ZINC	0.667	229.4 Da LogP 3.32 TPSA 63.3	✓ Ro5	✓ Clean	`CCCCCCCCCCC[C@@H](N)C(=O)O`
ZINC128850 ZINC	0.656	292.1 Da LogP 2.09 TPSA 35.5	✓ Ro5	✓ Clean	`COC(=O)c1ccc(OC)c(I)c1`
ZINC140445837 ZINC	0.656	294.1 Da LogP 2.37 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(S)c(I)c1`
ZINC21304461 ZINC	0.656	296.5 Da LogP 2.73 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(Cl)c(I)c1`
ZINC2506007 ZINC	0.656	246.4 Da LogP 4.00 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1ccc(C(C)(C)C)cc1`
ZINC393290 ZINC	0.656	277.1 Da LogP 1.66 TPSA 52.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(N)c(I)c1`
ZINC4069950 ZINC	0.656	220.3 Da LogP 2.71 TPSA 48.1	✓ Ro5	✓ Clean	`COc1ccc(-c2nc(N)sc2C)cc1`
ZINC44172055 ZINC	0.656	280.0 Da LogP 2.22 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(F)c(I)c1`
ZINC89064429 ZINC	0.656	340.9 Da LogP 2.84 TPSA 26.3	✓ Ro5	✓ Clean	`COC(=O)c1ccc(Br)c(I)c1`
ZINC38888013 ZINC	0.655	403.9 Da LogP 2.39 TPSA 46.5	✓ Ro5	✓ Clean	`COC(=O)c1cc(I)c(O)c(I)c1`
ZINC40162867 ZINC	0.655	254.2 Da LogP 3.88 TPSA 12.9	✓ Ro5	✓ Clean	`Cc1sc(Br)nc1-c1ccccc1`
ZINC150355 ZINC	0.647	224.7 Da LogP 3.35 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1cccc(Cl)c1`
ZINC41656350 ZINC	0.647	208.3 Da LogP 2.84 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1cccc(F)c1`
ZINC84915946 ZINC	0.647	269.2 Da LogP 3.46 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1sc(N)nc1-c1cccc(Br)c1`
ZINC404023 ZINC	0.645	210.2 Da LogP 0.97 TPSA 72.8	✓ Ro5	✓ Clean	`COC(=O)c1ccc(O)c(C(=O)OC)c1`
ZINC2471419 ZINC	0.636	266.4 Da LogP 4.37 TPSA 38.9	✓ Ro5	✓ Clean	`Cc1ccc(-c2nc(N)sc2-c2ccccc2)cc1`
ZINC39951739 ZINC	0.636	290.1 Da LogP 2.64 TPSA 26.3	✓ Ro5	✓ Clean	`CCc1ccc(C(=O)OC)cc1I`
ZINC39951741 ZINC	0.636	291.1 Da LogP 2.12 TPSA 38.3	✓ Ro5	✓ Clean	`CNc1ccc(C(=O)OC)cc1I`

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_2800

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