Protein target profile

VK055_5044

hisD

Genome: KpATCC43816 Gene: AIK83570.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 3 reactions UniProt A0A0H3GQM4

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Length 434

Pocket druggability 0.866

Metabolic reactions 3

Chokepoint No

Direct ligand evidence 0 81 total records

Functional annotation 1 EC 8 GO

Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Central metabolic position More central than 95.7% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. No similar human protein detected The current BLAST sequence screen did not find a significant human match, lowering apparent off-target risk. 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: No hit
Gut microbiome similarity: 9.8% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): Y
DEG identity (%): 43.939 Higher values support similarity to known essential genes.
DEG E-value: 1.13e-91 Smaller values mean stronger essential-gene similarity.

Localization

Localization: Cytoplasmic

Structure confidence

ColabFold pLDDT: 96.75 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

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 0.866

Structure A0A0H3GQM4

Pocket Pocket 1

P2Rank 0.955

Structure A0A0H3GQM4

Pocket Pocket 1

ColabFold model

FPocket 0.84 · Pocket 8

P2Rank 0.951 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 467 / 4744 genomes with a hit

Prevalence 9.8%

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 95.7% of genes in this genome, no human homolog detected.

Relative network centrality 95.7% more central than 95.7% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MSFNTIIDWNGCSADQQQQLLTRPAISASDSISKTVTEILNNVKANGDAALREYSAKFDKTTVAALQVSEAEIAAAGERLSDELKQAMAVAVKNIETFHNAQQLQAVDVETLPGVRCQQVTRPIASVGLYIPGGSAPLFSTVLMLATPARIAGCQQVVLCSPPPIADEILYAAQLCGVKTIFNVGGAQAIAALALGTESVPKVDKIFGPGNAYVTEAKRQVSQRLDGAAIDMPAGPSEVLVIADSGANPDFVASDLLSQAEHGPDSQVILLTPDADMGSRVAEAVERQLAALPRAETARVALSASRIIVARDLAQCVAISNQYGPEHLIIQTRQARELVDSITSAGSVFLGDWSPESAGDYASGTNHVLPTYGYTATCSSLGLADFQKRMTVQELSRDGFAALASTIEILAAAERLDAHKNAVTLRVAALKEQA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1.1.1.23

Gene Ontology (GO)

GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
GO:0051287 Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
GO:0046872 Binding to a metal ion.
GO:0000105 The chemical reactions and pathways resulting in the formation of L-histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid.
GO:0004399 Catalysis of the reaction: H2O + L-histidinol + 2 NAD+ = 3 H+ + L-histidine + 2 NADH.
GO:0016616 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
GO:0008270 Binding to a zinc ion (Zn).

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

38 records

Show feature table

Start	End	DB	Term	Name
6	427	SUPERFAMILY	SSF53720	ALDH-like
6	427	InterPro	IPR016161	Aldehyde/histidinol dehydrogenase
36	426	NCBIfam	TIGR00069	histidinol dehydrogenase
36	426	InterPro	IPR012131	Histidinol dehydrogenase
33	388	Gene3D	G3DSA:3.40.50.1980	Nitrogenase molybdenum iron protein domain
236	381	Gene3D	G3DSA:3.40.50.1980	Nitrogenase molybdenum iron protein domain
106	426	Gene3D	G3DSA:1.20.5.1300	-
7	428	Hamap	MF_01024	Histidinol dehydrogenase [hisD].
7	428	InterPro	IPR012131	Histidinol dehydrogenase
35	239	FunFam	G3DSA:3.40.50.1980:FF:000002	Histidinol dehydrogenase, chloroplastic
1	430	PIRSF	PIRSF000099	Histidinol_dh
1	430	InterPro	IPR022695	Histidinol dehydrogenase, monofunctional
383	427	FunFam	G3DSA:1.20.5.1300:FF:000001	Histidine biosynthesis trifunctional protein
28	427	Pfam	PF00815	Histidinol dehydrogenase
28	427	InterPro	IPR012131	Histidinol dehydrogenase
8	431	PANTHER	PTHR21256	HISTIDINOL DEHYDROGENASE HDH
8	431	InterPro	IPR012131	Histidinol dehydrogenase
109	136	PRINTS	PR00083	Histidinol dehydrogenase signature
109	136	InterPro	IPR012131	Histidinol dehydrogenase
198	223	PRINTS	PR00083	Histidinol dehydrogenase signature
198	223	InterPro	IPR012131	Histidinol dehydrogenase
36	60	PRINTS	PR00083	Histidinol dehydrogenase signature
36	60	InterPro	IPR012131	Histidinol dehydrogenase
168	194	PRINTS	PR00083	Histidinol dehydrogenase signature
168	194	InterPro	IPR012131	Histidinol dehydrogenase
361	379	PRINTS	PR00083	Histidinol dehydrogenase signature
361	379	InterPro	IPR012131	Histidinol dehydrogenase
230	251	PRINTS	PR00083	Histidinol dehydrogenase signature
230	251	InterPro	IPR012131	Histidinol dehydrogenase
252	271	PRINTS	PR00083	Histidinol dehydrogenase signature
252	271	InterPro	IPR012131	Histidinol dehydrogenase
320	345	PRINTS	PR00083	Histidinol dehydrogenase signature
320	345	InterPro	IPR012131	Histidinol dehydrogenase
240	378	FunFam	G3DSA:3.40.50.1980:FF:000001	Histidinol dehydrogenase
32	419	CDD	cd06572	Histidinol_dh
32	419	InterPro	IPR012131	Histidinol dehydrogenase
230	262	ProSitePatterns	PS00611	Histidinol dehydrogenase signature.
230	262	InterPro	IPR001692	Histidinol dehydrogenase, conserved 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 #1

0.866

Likely same site as P2Rank 1 0.8 Å 33 shared residues 94% of smaller site

Unusual size

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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

0.955

Likely same site as FPocket 1 0.8 Å 33 shared residues 94% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.061

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Surrounding area

Site 3 P2Rank #3

0.003

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Surrounding area

Residue sets

UniProt: Active site:326-326 Proton acceptor

UniProt: Active site:327-327 Proton acceptor

UniProt: Binding site:130-130

UniProt: Binding site:188-188

UniProt: Binding site:211-211

UniProt: Binding site:237-237

UniProt: Binding site:259-259

UniProt: Binding site:262-262

UniProt: Binding site:327-327

UniProt: Binding site:360-360

UniProt: Binding site:414-414

UniProt: Binding site:419-419

Binding pockets · P2Rank

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

Site 1 P2Rank #1

0.951

Likely same site as FPocket 8 1.1 Å 33 shared residues 89% of smaller site

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Surrounding area

Site 2 P2Rank #2

0.133

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Surrounding area

Site 3 P2Rank #3

0.053

Show in viewer

Surrounding area

Residue sets

UniProt: Active site:326-326 Proton acceptor

UniProt: Active site:327-327 Proton acceptor

UniProt: Binding site:130-130

UniProt: Binding site:188-188

UniProt: Binding site:211-211

UniProt: Binding site:237-237

UniProt: Binding site:259-259

UniProt: Binding site:262-262

UniProt: Binding site:327-327

UniProt: Binding site:360-360

UniProt: Binding site:414-414

UniProt: Binding site:419-419

All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

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
AlphaFold DB AF_A0A0H3GQM4	AlphaFold DB	—	—	full sequence	—	Viewing
ColabFold VK055_5044	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.

81 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 31 records from similar proteins

Structural ligands 3 0 loaded crystals

Measured bioactivity 28 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

0VD PDB via homolog 335.4 Da · LogP 2.67 · TPSA 81.0 Open detail RCSB PDB

HSM PDB via homolog Detail RCSB PDB

HSO PDB via homolog Detail RCSB PDB

CHEMBL307302 ChEMBL via homolog · pchembl 8.85 (~1.4 nM) Detail ChEMBL

CHEMBL477469 ChEMBL via homolog · pchembl 8.52 (~3.0 nM) Detail ChEMBL

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
0VD RCSB PDB	4G09	Q8G2R2	335.4 Da LogP 2.67 TPSA 81.0	✓ Ro5	✓ Clean	`c1ccc(cc1)COc2ccc(cc2)CC(=O)[C@H](Cc3c[nH]cn3)N`
HSM RCSB PDB	1KAR	P06988	111.1 Da LogP -0.09 TPSA 54.7	✓ Ro5	✓ Clean	`c1c(nc[nH]1)CCN`
HSO RCSB PDB	5VLC	G7IKX3	142.2 Da LogP -1.31 TPSA 76.2	✓ Ro5	✓ Clean	`c1c([nH+]c[nH]1)C[C@@H](CO)N`

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
CHEMBL307302 ChEMBL	P06988	8.85 ~1.4 nM	139.2 Da LogP -0.52 TPSA 71.8	✓ Ro5	✓ Clean	`N[C@H](C=O)Cc1c[nH]cn1`
CHEMBL477469 ChEMBL	Q8G2R2	8.52 ~3.0 nM	408.3 Da LogP 3.51 TPSA 81.0	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(OCc2ccccc…`
CHEMBL476671 ChEMBL	Q8G2R2	8.22 ~6.0 nM	392.2 Da LogP 2.63 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1c(F)c(F)c(F)c…`
CHEMBL477467 ChEMBL	Q8G2R2	8.22 ~6.0 nM	332.2 Da LogP 1.94 TPSA 81.0	✓ Ro5	✓ Clean	`COc1ccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)cc1.Cl.Cl`
CHEMBL477468 ChEMBL	Q8G2R2	8.22 ~6.0 nM	394.3 Da LogP 3.73 TPSA 81.0	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Oc2ccccc2…`
CHEMBL477470 ChEMBL	Q8G2R2	8.22 ~6.0 nM	338.2 Da LogP 2.21 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(F)cc1F`
CHEMBL477653 ChEMBL	Q8G2R2	8.22 ~6.0 nM	352.3 Da LogP 3.09 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1cccc2ccccc12`
CHEMBL477654 ChEMBL	Q8G2R2	8.22 ~6.0 nM	352.3 Da LogP 3.09 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc2ccccc2c1`
CHEMBL477655 ChEMBL	Q8G2R2	8.22 ~6.0 nM	346.2 Da LogP 1.66 TPSA 90.2	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc2c(c1)OCO2`
CHEMBL477675 ChEMBL	Q8G2R2	8.22 ~6.0 nM	371.1 Da LogP 3.24 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Cl)c(Cl)c1`
CHEMBL478080 ChEMBL	Q8G2R2	8.22 ~6.0 nM	316.2 Da LogP 2.24 TPSA 71.8	✓ Ro5	✓ Clean	`Cc1ccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)cc1.Cl.Cl`
CHEMBL483666 ChEMBL	Q8G2R2	8.22 ~6.0 nM	320.2 Da LogP 2.07 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(F)cc1`
CHEMBL483667 ChEMBL	Q8G2R2	8.22 ~6.0 nM	381.1 Da LogP 2.70 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Br)cc1`
CHEMBL483668 ChEMBL	Q8G2R2	8.22 ~6.0 nM	378.3 Da LogP 3.60 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(-c2ccccc2…`
CHEMBL500316 ChEMBL	Q8G2R2	8.22 ~6.0 nM	302.2 Da LogP 1.93 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccccc1`
CHEMBL553052 ChEMBL	P24226	8.13 ~7.4 nM	317.2 Da LogP 1.52 TPSA 97.8	✓ Ro5	✓ Clean	`Cl.Cl.Nc1cccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)c1`
CHEMBL3215563 ChEMBL	Q8G2R2	7.70 ~20.0 nM	444.0 Da LogP 4.09 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Cl)…`
CHEMBL3219295 ChEMBL	Q8G2R2	7.61 ~24.5 nM	205.6 Da LogP -0.74 TPSA 92.0	✓ Ro5	✓ Clean	`Cl.N[C@@H](Cc1c[nH]cn1)C(=O)CO`
CHEMBL555499 ChEMBL	P24226	7.30 ~50.1 nM	460.0 Da LogP 3.46 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Br)c(Br)c1`
CHEMBL540286 ChEMBL	P24226	7.00 ~100.0 nM	381.1 Da LogP 2.70 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1cccc(Br)c1`
CHEMBL3219299 ChEMBL	Q8G2R2	6.97 ~107.2 nM	331.8 Da LogP 2.50 TPSA 81.0	✓ Ro5	✓ Clean	`Cl.N[C@@H](Cc1c[nH]cn1)C(=O)COc1ccc2ccccc2c1`
CHEMBL3219297 ChEMBL	Q8G2R2	6.68 ~208.9 nM	295.8 Da LogP 1.66 TPSA 81.0	✓ Ro5	✓ Clean	`Cc1ccc(OCC(=O)[C@@H](N)Cc2c[nH]cn2)cc1.Cl`
CHEMBL519986 ChEMBL	P24226	6.52 ~302.0 nM	336.7 Da LogP 2.59 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccc(Cl)cc1`
CHEMBL553218 ChEMBL	P24226	6.52 ~302.0 nM	318.2 Da LogP 1.64 TPSA 92.0	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1cccc(O)c1`
CHEMBL538257 ChEMBL	P24226	6.30 ~501.2 nM	317.2 Da LogP 1.52 TPSA 97.8	✓ Ro5	Alert	`Cl.Cl.Nc1ccc(CC(=O)[C@@H](N)Cc2c[nH]cn2)cc1`
CHEMBL543341 ChEMBL	P24226	6.00 ~1.0 µM	381.1 Da LogP 2.70 TPSA 71.8	✓ Ro5	✓ Clean	`Cl.Cl.N[C@@H](Cc1c[nH]cn1)C(=O)Cc1ccccc1Br`
AZM ChEMBL	Q8G2R2	—	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(s1)S(=O)(=O)N`
CHEMBL1093178 ChEMBL	Q8G2R2	—	318.4 Da LogP -1.43 TPSA 142.1	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(S(N)(=O)=O)cc2)[C@@H](O)[…`

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
ZINC3813042 ZINC	1.000	222.3 Da LogP -0.86 TPSA 115.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC1634512 ZINC	0.719	221.3 Da LogP -0.10 TPSA 89.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(C)(=O)=O)s1`
ZINC72188049 ZINC	0.719	223.2 Da LogP -0.26 TPSA 109.3	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)O)s1`
ZINC225947763 ZINC	0.706	238.2 Da LogP -0.64 TPSA 124.3	✓ Ro5	✓ Clean	`COC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC5353439 ZINC	0.706	237.3 Da LogP -1.06 TPSA 127.1	✓ Ro5	✓ Clean	`CNC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC77273327 ZINC	0.697	427.5 Da LogP -1.03 TPSA 190.1	1 viol.	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NS(=O)(=O)c2nnc(NC(C)=O)s…`
ZINC4217364 ZINC	0.686	236.3 Da LogP -0.47 TPSA 115.0	✓ Ro5	✓ Clean	`CCC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC2522680 ZINC	0.682	245.3 Da LogP 1.02 TPSA 81.0	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)OCc1ccccc1`
ZINC29253676 ZINC	0.676	236.3 Da LogP -0.60 TPSA 101.1	✓ Ro5	✓ Clean	`CNS(=O)(=O)c1nnc(NC(C)=O)s1`
ZINC299872822 ZINC	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC299872823 ZINC	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC299872824 ZINC	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC3995728 ZINC	0.658	476.5 Da LogP -0.17 TPSA 163.9	1 viol.	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(-c3ccc(N[C@@H]4O[C@H](C)[…`
ZINC101133776 ZINC	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@@H](O)[C@H…`
ZINC253615125 ZINC	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@H](O)[C@H]…`
ZINC253615126 ZINC	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@H](O)[C@@H…`
ZINC25664323 ZINC	0.651	304.3 Da LogP -1.82 TPSA 142.1	✓ Ro5	✓ Clean	`NS(=O)(=O)c1ccc(N[C@@H]2O[C@H](CO)[C@@H](O)[C@@…`
ZINC32150186 ZINC	0.649	250.3 Da LogP -0.08 TPSA 115.0	✓ Ro5	✓ Clean	`CCCC(=O)Nc1nnc(S(N)(=O)=O)s1`
ZINC245333872 ZINC	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@@H](O)[…`
ZINC245333873 ZINC	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@@H](O)[…`
ZINC245333874 ZINC	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@H](O)[C…`
ZINC245333875 ZINC	0.625	318.2 Da LogP 0.69 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Br)cc2)[C@H](O)[C@H](O)[C…`
ZINC584904325 ZINC	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@@H](O)[…`
ZINC584904326 ZINC	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@@H](O)[…`
ZINC584904327 ZINC	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@H](O)[C…`
ZINC584904328 ZINC	0.625	273.7 Da LogP 0.58 TPSA 82.0	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(Cl)cc2)[C@H](O)[C@H](O)[C…`
ZINC36182508 ZINC	0.622	264.3 Da LogP 0.18 TPSA 101.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NC(C)C)s1`
ZINC5160987 ZINC	0.622	278.4 Da LogP 0.57 TPSA 101.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NC(C)(C)C)s1`
ZINC1709589 ZINC	0.621	200.2 Da LogP 0.45 TPSA 84.0	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(NC(C)=O)s1`
ZINC101308421 ZINC	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@H](O)[C…`
ZINC1204694 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@H](…`
ZINC1856103 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@H](…`
ZINC239432830 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@@H]…`
ZINC239432831 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@@H]…`
ZINC239433127 ZINC	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@@H](O)[…`
ZINC239433128 ZINC	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@@H](O)[…`
ZINC3999200 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@H…`
ZINC3999201 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@…`
ZINC3999202 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@H…`
ZINC3999203 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@@H](Nc2ccc(C(=O)O)cc2)[C@@H](O)[C@@…`
ZINC4092845 ZINC	0.619	281.3 Da LogP 0.13 TPSA 99.0	✓ Ro5	✓ Clean	`CC(=O)c1ccc(N[C@@H]2O[C@H](C)[C@H](O)[C@H](O)[C…`
ZINC5587198 ZINC	0.619	283.3 Da LogP -0.38 TPSA 119.3	✓ Ro5	✓ Clean	`C[C@@H]1O[C@H](Nc2ccc(C(=O)O)cc2)[C@H](O)[C@H](…`
ZINC2575496 ZINC	0.612	302.3 Da LogP 0.09 TPSA 121.1	✓ Ro5	✓ Clean	`N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1ccccc1)C(=O…`
ZINC36182715 ZINC	0.605	278.4 Da LogP 0.53 TPSA 92.3	✓ Ro5	✓ Clean	`CCN(CC)S(=O)(=O)c1nnc(NC(C)=O)s1`
ZINC5925089 ZINC	0.605	280.3 Da LogP -1.01 TPSA 152.3	✓ Ro5	✓ Clean	`NS(=O)(=O)c1nnc(NC(=O)CCC(=O)O)s1`
ZINC54788510 ZINC	0.595	201.3 Da LogP 1.52 TPSA 54.7	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccccc1)Cc1c[nH]cn1`
ZINC54788511 ZINC	0.595	201.3 Da LogP 1.52 TPSA 54.7	✓ Ro5	✓ Clean	`N[C@H](Cc1ccccc1)Cc1c[nH]cn1`
ZINC36182505 ZINC	0.590	264.3 Da LogP 0.18 TPSA 101.1	✓ Ro5	✓ Clean	`CCCNS(=O)(=O)c1nnc(NC(C)=O)s1`
ZINC36182511 ZINC	0.590	262.3 Da LogP -0.06 TPSA 101.1	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)NC2CC2)s1`
ZINC36182529 ZINC	0.590	276.3 Da LogP 0.28 TPSA 92.3	✓ Ro5	✓ Clean	`CC(=O)Nc1nnc(S(=O)(=O)N2CCCC2)s1`

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_5044

Strong target candidate with converging metabolic, structural and chemical evidence.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Chemistry

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