Protein target profile

VK055_2229

alkaline phosphatase H

Genome: KpATCC43816 Gene: AIK80834.1 phoA 3D evidence: Experimental + ColabFold model Metabolism 18 reactions UniProt A0A0H3GK94

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Length 471

Pocket druggability 0.23

Metabolic reactions 18

Chokepoint No

Direct ligand evidence 0 84 total records

Functional annotation 1 EC 4 GO

Target summary

Target candidate with partial support; inspect missing evidence before prioritizing.

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. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Structure available Experimental + ColabFold model Ligand evidence via structure/bioactivity 7 structural and 27 bioactivity records.

Risks to review

Human similarity Top human hit identity: 30.362%. Microbiome similarity 116 of 4744 screened genomes (2.4%) have a significant similarity hit. Weak predicted binding pocket FPocket selected-pocket score 0.23. Weak second pocket-predictor signal P2Rank predicted binding-site probability 0.24.

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 (%): 30.362 Lower values reduce human off-target concern.
Human E-value: 2.1000000000000002e-29
Gut microbiome similarity: 2.4% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG): N
DEG identity (%): 36.31 Higher values support similarity to known essential genes.

Localization

Localization: Periplasmic

Structure confidence

ColabFold pLDDT: 93.84 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 0.23

Structure 7TM9

Pocket Pocket 2

P2Rank 0.244

Structure 7TM9

Pocket Pocket 1

ColabFold model

FPocket 0.253 · Pocket 7

P2Rank 0.559 · Pocket 1

Core conservation Conserved core gene

Roary core

CoreCruncher core

Gut microbiome 116 / 4744 genomes with a hit

Prevalence 2.4%

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

Relative network centrality 0.0% more central than 0.0% of genes in this genome

Chokepoint Not a chokepoint

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MKLSALFIALIPLLGSPVIHAETTAAPVLENRAAQGDITTPGGARRLTGDQTEALRASLINKPAKNVILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYSLDKKTGKPDYVTDSAASATAWTTGVKTYNGALGVDIHENAHQTILELAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPTVTSEKCPSNALEKGGKGSITEQLLNARPDVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQIVTDAASLAAATEASQDKPLLGLFADGNMPVRWEGPKASYHGNIDKPPVTCTPNPKRDASVPTLAQMTEKAIDLLSRNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQKALEFARKDGNTLVIVTADHAHASQIIPADSKAPGLTQALNTHDGAVMVMSYGNSEEESMEHTGTQLRIAAYGPHAANVVGLTDQTDLFTTMKAALSLK

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

3.1.3.1

Gene Ontology (GO)

GO:0016791 Catalysis of the hydrolysis of a phosphoric monoester, releasing a phosphate.
GO:0042597 The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).
GO:0004035 Catalysis of the reaction: a phosphate monoester + H2O = an alcohol + phosphate, with an alkaline pH optimum.
GO:0046872 Binding to a metal ion.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

32 records

Show feature table

Start	End	DB	Term	Name
22	471	Phobius	NON_CYTOPLASMIC_DOMAIN	Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
15	21	Phobius	SIGNAL_PEPTIDE_C_REGION	C-terminal region of a signal peptide.
65	468	CDD	cd16012	ALP
65	468	InterPro	IPR001952	Alkaline phosphatase
23	471	Gene3D	G3DSA:3.40.720.10	Alkaline Phosphatase, subunit A
23	471	InterPro	IPR017850	Alkaline-phosphatase-like, core domain superfamily
1	21	SignalP_EUK	SignalP-noTM	SignalP-noTM
1	2	Phobius	SIGNAL_PEPTIDE_N_REGION	N-terminal region of a signal peptide.
121	136	PRINTS	PR00113	Alkaline phosphatase signature
121	136	InterPro	IPR001952	Alkaline phosphatase
320	349	PRINTS	PR00113	Alkaline phosphatase signature
320	349	InterPro	IPR001952	Alkaline phosphatase
64	84	PRINTS	PR00113	Alkaline phosphatase signature
64	84	InterPro	IPR001952	Alkaline phosphatase
221	231	PRINTS	PR00113	Alkaline phosphatase signature
221	231	InterPro	IPR001952	Alkaline phosphatase
158	178	PRINTS	PR00113	Alkaline phosphatase signature
158	178	InterPro	IPR001952	Alkaline phosphatase
65	471	SMART	SM00098	alk_phosph_2
65	471	InterPro	IPR001952	Alkaline phosphatase
64	431	Pfam	PF00245	Alkaline phosphatase
64	431	InterPro	IPR001952	Alkaline phosphatase
25	469	PANTHER	PTHR11596	ALKALINE PHOSPHATASE
25	469	InterPro	IPR001952	Alkaline phosphatase
23	471	FunFam	G3DSA:3.40.720.10:FF:000040	Alkaline phosphatase
37	470	SUPERFAMILY	SSF53649	Alkaline phosphatase-like
37	470	InterPro	IPR017850	Alkaline-phosphatase-like, core domain superfamily
3	14	Phobius	SIGNAL_PEPTIDE_H_REGION	Hydrophobic region of a signal peptide.
121	129	ProSitePatterns	PS00123	Alkaline phosphatase active site.
121	129	InterPro	IPR018299	Alkaline phosphatase, active site
1	21	SignalP_GRAM_POSITIVE	SignalP-TM	SignalP-TM
1	21	Phobius	SIGNAL_PEPTIDE	Signal peptide region

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 #2

0.23

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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

0.244

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Surrounding area

Site 2 P2Rank #2

0.018

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Surrounding area

Site 3 P2Rank #3

0.015

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Surrounding area

Site 4 P2Rank #4

0.006

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Surrounding area

Site 5 P2Rank #5

0.003

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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

0.559

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Surrounding area

Site 2 P2Rank #2

0.065

Likely same site as FPocket 7 1.5 Å 12 shared residues 86% of smaller site

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Surrounding area

Site 3 P2Rank #3

0.031

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Surrounding area

Site 4 P2Rank #4

0.017

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Surrounding area

Site 5 P2Rank #5

0.014

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Surrounding area

Residue sets

UniProt: Active site:129-129 Phosphoserine intermediate

UniProt: Binding site:129-129

UniProt: Binding site:180-180

UniProt: Binding site:182-182

UniProt: Binding site:349-349

UniProt: Binding site:354-354

UniProt: Binding site:358-358

UniProt: Binding site:396-396

UniProt: Binding site:397-397

UniProt: Binding site:439-439

UniProt: Binding site:78-78

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 7TM9	X-ray	1.95 Å	A,B,C,D,E,F,G,H	95.8% 21-471	PDBe RCSB PDBj File	Viewing
ColabFold VK055_2229	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.

84 records

Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records

Transferred evidence 34 records from similar proteins

Structural ligands 7 0 loaded crystals

Measured bioactivity 27 direct and transferred ChEMBL records

Proposed compounds 50 similarity-based ZINC candidates

Best available ligand signal

4NP PDB via homolog 219.1 Da · LogP 1.07 · TPSA 109.9 Open detail RCSB PDB

AF3 PDB via homolog Detail RCSB PDB

HAI PDB via homolog Detail RCSB PDB

MMQ PDB via homolog Detail RCSB PDB

NPO 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
4NP RCSB PDB	4KJG	P15693	219.1 Da LogP 1.07 TPSA 109.9	✓ Ro5	✓ Clean	`c1cc(ccc1[N+](=O)[O-])OP(=O)(O)O`
AF3 RCSB PDB	1KHJ	P00634	84.0 Da LogP 0.88 TPSA 0.0	✓ Ro5	✓ Clean	`F[Al](F)F`
HAI RCSB PDB	6T26	Q93P54	100.2 Da LogP 0.56 TPSA 27.6	✓ Ro5	✓ Clean	`C1CCC(CC1)[NH3+]`
MMQ RCSB PDB	1EW9	P00634	126.1 Da LogP -1.21 TPSA 63.2	✓ Ro5	✓ Clean	`C(P(=O)([O-])[O-])S`
NPO RCSB PDB	3MK0	P05187	139.1 Da LogP 1.30 TPSA 63.4	✓ Ro5	✓ Clean	`c1cc(ccc1[N+](=O)[O-])O`
PAE RCSB PDB	1EW8	P00634	140.0 Da LogP -0.75 TPSA 94.8	✓ Ro5	✓ Clean	`C(C(=O)O)P(=O)(O)O`
WO4 RCSB PDB	5C66	P00634	247.8 Da LogP -2.62 TPSA 80.3	✓ Ro5	✓ Clean	`[O-][W](=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).

Ligand	UniProt (homolog)	pchembl	MW · LogP · TPSA	Lipinski	PAINS	SMILES
CHEMBL5173145 ChEMBL	P05187	7.50 ~31.6 nM	514.4 Da LogP 5.39 TPSA 117.5	2 viol.	✓ Clean	`COc1c(Cl)cc(-c2cccc(C[C@@H](NC(=O)c3cc(-c4ccc(C…`
CHEMBL559431 ChEMBL	P10696	7.22 ~60.3 nM	441.7 Da LogP 6.13 TPSA 30.5	1 viol.	✓ Clean	`CO[C@@H]1CC[C@@]2(C)[C@H](CC[C@H]3[C@@H]4CC[C@@…`
CHEMBL5820397 ChEMBL	P10696	7.22 ~60.3 nM	510.8 Da LogP 5.53 TPSA 58.6	2 viol.	✓ Clean	`CC(=O)NCCN1C[C@@H](C)C[C@H]2O[C@]3(CC[C@@H]4C(=…`
CHEMBL5874649 ChEMBL	P10696	7.22 ~60.3 nM	709.0 Da LogP 8.86 TPSA 77.1	2 viol.	✓ Clean	`CC1=C2C[C@H]3[C@@H](CC[C@@H]4C[C@H](OC(=O)CNCc5…`
CHEMBL5893768 ChEMBL	P10696	7.22 ~60.3 nM	561.8 Da LogP 7.52 TPSA 59.0	2 viol.	✓ Clean	`CC1=C2C[C@H]3[C@@H](CC[C@@H]4C[C@@H](O)CC[C@@]4…`
CHEMBL6055533 ChEMBL	P10696	7.22 ~60.3 nM	561.8 Da LogP 7.52 TPSA 59.0	2 viol.	✓ Clean	`CC1=C2C[C@H]3[C@@H](CC[C@@H]4C[C@H](O)CC[C@@]43…`
CHEMBL1302272 ChEMBL	P10696	6.69 ~204.2 nM	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc(C2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
CHEMBL1734721 ChEMBL	P10696	6.43 ~371.5 nM	296.3 Da LogP 2.22 TPSA 81.6	✓ Ro5	Alert	`O=C1Nc2ccccc2/C1=C\NCCc1ccc(O)c(O)c1`
CHEMBL1336276 ChEMBL	P10696	6.34 ~457.1 nM	433.5 Da LogP 1.83 TPSA 101.6	✓ Ro5	✓ Clean	`O=C(Cn1c(=O)oc2cc(S(=O)(=O)N3CCCC3)ccc21)NCc1cc…`
CHEMBL1300370 ChEMBL	P10696	6.26 ~549.5 nM	332.2 Da LogP 2.56 TPSA 62.4	✓ Ro5	✓ Clean	`O=C1Nc2ccc(Br)cc2C12NNc1ccccc1O2`
CHEMBL592869 ChEMBL	P10696	6.22 ~602.6 nM	290.3 Da LogP 2.48 TPSA 83.3	✓ Ro5	Alert	`Cc1cc(C)nc(SCC(=O)c2ccc(O)c(O)c2)n1`
CHEMBL1476029 ChEMBL	P10696	6.18 ~660.7 nM	293.3 Da LogP 4.65 TPSA 70.1	✓ Ro5	Alert	`C=CCn1c(O)c(N=Nc2ccccc2O)c2ccccc21`
CHEMBL1505198 ChEMBL	P10696	6.14 ~724.4 nM	293.3 Da LogP 2.38 TPSA 53.6	✓ Ro5	✓ Clean	`C=CCN1C(=O)C2(NNc3ccccc3O2)c2ccccc21`
CHEMBL5171390 ChEMBL	P05187	—	587.0 Da LogP 5.18 TPSA 132.0	2 viol.	✓ Clean	`CC(C)(C)OC(=O)n1c(-c2ccccc2C[C@@H](NC(=O)c2cnc3…`
CHEMBL5173448 ChEMBL	P05187	—	530.9 Da LogP 5.57 TPSA 95.5	2 viol.	✓ Clean	`Cc1ccc2c(c1)NC(=O)C2CC(=O)N[C@@H](Cc1ccc(-c2ccc…`
CHEMBL5175183 ChEMBL	P05187	—	752.0 Da LogP 1.93 TPSA 226.1	2 viol.	✓ Clean	`C[C@@H]1CCC[C@H](C)N1CCC(=O)N[C@@H](CCC(=O)N[C@…`
CHEMBL5179108 ChEMBL	P05187	—	587.0 Da LogP 5.18 TPSA 132.0	2 viol.	✓ Clean	`CC(C)(C)OC(=O)n1c(-c2ccccc2C[C@H](NC(=O)c2cnc3c…`
CHEMBL5183101 ChEMBL	P05187	—	552.4 Da LogP 3.40 TPSA 125.4	1 viol.	✓ Clean	`Cc1ccc(NC(=O)NCC#Cc2ccc(C[C@@H](NC(=O)c3nn(C)c(…`
CHEMBL5185903 ChEMBL	P05187	—	688.7 Da LogP 3.06 TPSA 233.1	2 viol.	Alert	`Cc1cc(-c2cnccn2)ccc1NC(=O)[C@@H](CCC(N)=O)n1cc(…`
CHEMBL5186116 ChEMBL	P05187	—	552.4 Da LogP 3.40 TPSA 125.4	1 viol.	✓ Clean	`Cc1ccc(NC(=O)NCC#Cc2ccc(C[C@H](NC(=O)c3nn(C)c(C…`
CHEMBL5187220 ChEMBL	P05187	—	688.7 Da LogP 4.09 TPSA 216.6	2 viol.	Alert	`NC(=O)CC[C@@H](C(=O)Nc1cccc(Oc2ccccc2)c1)n1cc(C…`
CHEMBL5190490 ChEMBL	P05187	—	688.7 Da LogP 4.09 TPSA 216.6	2 viol.	Alert	`NC(=O)CC[C@H](C(=O)Nc1cccc(Oc2ccccc2)c1)n1cc(CN…`
CHEMBL5198097 ChEMBL	P05187	—	545.0 Da LogP 5.66 TPSA 84.5	2 viol.	✓ Clean	`COC(=O)[C@H](Cc1ccc(-c2ccc(Cl)cc2C(F)(F)F)cc1)N…`
CHEMBL5199784 ChEMBL	P05187	—	688.7 Da LogP 3.06 TPSA 233.1	2 viol.	Alert	`Cc1cc(-c2cnccn2)ccc1NC(=O)[C@H](CCC(N)=O)n1cc(C…`
CHEMBL5200679 ChEMBL	P05187	—	514.4 Da LogP 5.39 TPSA 117.5	2 viol.	✓ Clean	`COc1c(Cl)cc(-c2cccc(C[C@H](NC(=O)c3cc(-c4ccc(C)…`
CHEMBL5203638 ChEMBL	P05187	—	679.9 Da LogP 1.70 TPSA 188.8	2 viol.	✓ Clean	`C[C@@H]1CCC[C@H](C)N1CCC(=O)N[C@@H](CCC(=O)NCC(…`
STL ChEMBL	P10696	—	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`c1cc(ccc1\C=C\c2cc(cc(c2)O)O)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
ZINC111949 ZINC	1.000	290.3 Da LogP 2.48 TPSA 83.3	✓ Ro5	Alert	`Cc1cc(C)nc(SCC(=O)c2ccc(O)c(O)c2)n1`
ZINC12353732 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2cc(O)cc(O)c2)cc1`
ZINC13756545 ZINC	1.000	296.3 Da LogP 2.22 TPSA 81.6	✓ Ro5	Alert	`O=C1Nc2ccccc2/C1=C\NCCc1ccc(O)c(O)c1`
ZINC1397695 ZINC	1.000	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc([C@H]2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
ZINC1397696 ZINC	1.000	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc([C@@H]2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
ZINC1397833 ZINC	1.000	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc(C2=NNC(=O)[C@@H](c3ccc(Cl)cc3)C2)cc1`
ZINC1397834 ZINC	1.000	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc(C2=NNC(=O)[C@H](c3ccc(Cl)cc3)C2)cc1`
ZINC1529638 ZINC	1.000	219.1 Da LogP 1.07 TPSA 109.9	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(OP(=O)(O)O)cc1`
ZINC1857524289 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2cc(O)cc(O)c2)cc1`
ZINC2297318797 ZINC	1.000	296.3 Da LogP 2.22 TPSA 81.6	✓ Ro5	Alert	`O=C1Nc2ccccc2C1=CNCCc1ccc(O)c(O)c1`
ZINC3416064 ZINC	1.000	332.2 Da LogP 2.56 TPSA 62.4	✓ Ro5	✓ Clean	`O=C1Nc2ccc(Br)cc2[C@]12NNc1ccccc1O2`
ZINC3416066 ZINC	1.000	332.2 Da LogP 2.56 TPSA 62.4	✓ Ro5	✓ Clean	`O=C1Nc2ccc(Br)cc2[C@@]12NNc1ccccc1O2`
ZINC6787 ZINC	1.000	228.2 Da LogP 2.97 TPSA 60.7	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(O)c2)cc1`
ZINC5794817 ZINC	0.861	278.4 Da LogP 3.31 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc(C2=NNC(=O)[C@H](c3ccc(C)cc3)C2)cc1`
ZINC5794866 ZINC	0.861	278.4 Da LogP 3.31 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1ccc(C2=NNC(=O)[C@@H](c3ccc(C)cc3)C2)cc1`
ZINC1397703 ZINC	0.800	302.7 Da LogP 3.49 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(Cl)cc2)C[C@@H]1c1ccc(F)cc1`
ZINC1397704 ZINC	0.800	302.7 Da LogP 3.49 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(Cl)cc2)C[C@H]1c1ccc(F)cc1`
ZINC1397707 ZINC	0.786	326.8 Da LogP 4.47 TPSA 41.5	✓ Ro5	✓ Clean	`CC(C)c1ccc([C@H]2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
ZINC1397708 ZINC	0.786	326.8 Da LogP 4.47 TPSA 41.5	✓ Ro5	✓ Clean	`CC(C)c1ccc([C@@H]2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
ZINC1529745 ZINC	0.786	340.2 Da LogP 3.06 TPSA 142.0	✓ Ro5	✓ Clean	`O=[N+]([O-])c1ccc(OP(=O)(O)Oc2ccc([N+](=O)[O-])…`
ZINC1397725 ZINC	0.780	363.6 Da LogP 4.11 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(Br)cc2)C[C@@H]1c1ccc(Cl)cc1`
ZINC1397726 ZINC	0.780	363.6 Da LogP 4.11 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(Br)cc2)C[C@H]1c1ccc(Cl)cc1`
ZINC113264413 ZINC	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC113264415 ZINC	0.778	317.4 Da LogP 3.98 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccc(-c3ccccc3)cc2)cc1)C(=O)O`
ZINC2244337 ZINC	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC2244338 ZINC	0.778	241.3 Da LogP 2.31 TPSA 63.3	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(-c2ccccc2)cc1)C(=O)O`
ZINC1834294 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@H](N)C(=O)O)c1)C(=O)O`
ZINC1834295 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC1834297 ZINC	0.769	252.3 Da LogP -0.40 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@H](Cc1cccc(C[C@@H](N)C(=O)O)c1)C(=O)O`
ZINC9691143 ZINC	0.769	304.4 Da LogP 2.79 TPSA 83.3	✓ Ro5	Alert	`Cc1nc(SCC(=O)c2ccc(O)c(O)c2)nc(C)c1C`
ZINC1397701 ZINC	0.767	312.8 Da LogP 3.91 TPSA 41.5	✓ Ro5	✓ Clean	`CCc1ccc([C@H]2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
ZINC1397702 ZINC	0.767	312.8 Da LogP 3.91 TPSA 41.5	✓ Ro5	✓ Clean	`CCc1ccc([C@@H]2CC(c3ccc(Cl)cc3)=NNC2=O)cc1`
ZINC100463064 ZINC	0.761	280.3 Da LogP 2.52 TPSA 61.4	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C/NCCc1ccc(O)cc1`
ZINC6231280 ZINC	0.761	280.3 Da LogP 2.52 TPSA 61.4	✓ Ro5	✓ Clean	`O=C1Nc2ccccc2/C1=C\NCCc1ccc(O)cc1`
ZINC51331930 ZINC	0.756	276.3 Da LogP 2.17 TPSA 83.3	✓ Ro5	Alert	`Cc1ccnc(SCC(=O)c2ccc(O)c(O)c2)n1`
ZINC1397705 ZINC	0.750	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1cccc(C2=NNC(=O)[C@@H](c3ccc(Cl)cc3)C2)c1`
ZINC1397706 ZINC	0.750	298.8 Da LogP 3.66 TPSA 41.5	✓ Ro5	✓ Clean	`Cc1cccc(C2=NNC(=O)[C@H](c3ccc(Cl)cc3)C2)c1`
ZINC1397719 ZINC	0.738	353.6 Da LogP 4.65 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(Cl)c(Cl)c2)C[C@@H]1c1ccc(Cl)cc1`
ZINC1397720 ZINC	0.738	353.6 Da LogP 4.65 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(Cl)c(Cl)c2)C[C@H]1c1ccc(Cl)cc1`
ZINC13319959 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C\c2ccc(O)cc2)cc1`
ZINC1510311 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2ccc(O)cc2)cc1`
ZINC1875408805 ZINC	0.737	212.2 Da LogP 3.27 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(C=Cc2ccc(O)cc2)cc1`
ZINC6519844 ZINC	0.733	217.1 Da LogP 1.79 TPSA 89.7	✓ Ro5	✓ Clean	`C[P@@](=O)(O)Oc1ccc([N+](=O)[O-])cc1`
ZINC39351856 ZINC	0.731	328.4 Da LogP 1.26 TPSA 126.6	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(-c2ccc(C[C@H](N)C(=O)O)cc2)cc1)C…`
ZINC11689625 ZINC	0.729	404.4 Da LogP 2.40 TPSA 89.6	✓ Ro5	✓ Clean	`O=C(Cn1c(=O)oc2cc(S(=O)(=O)N3CCCC3)ccc21)c1ccc(…`
ZINC1403202 ZINC	0.727	352.7 Da LogP 4.37 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(C(F)(F)F)cc2)C[C@@H]1c1ccc(Cl)cc1`
ZINC1403203 ZINC	0.727	352.7 Da LogP 4.37 TPSA 41.5	✓ Ro5	✓ Clean	`O=C1NN=C(c2ccc(C(F)(F)F)cc2)C[C@H]1c1ccc(Cl)cc1`
ZINC2561081 ZINC	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC2561082 ZINC	0.724	269.3 Da LogP 1.87 TPSA 80.4	✓ Ro5	✓ Clean	`N[C@@H](Cc1ccc(C(=O)c2ccccc2)cc1)C(=O)O`
ZINC34544488 ZINC	0.720	230.2 Da LogP 3.41 TPSA 40.5	✓ Ro5	✓ Clean	`Oc1ccc(/C=C/c2cc(O)cc(F)c2)cc1`

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_2229

Target candidate with partial support; inspect missing evidence before prioritizing.

Main supporting evidence

Risks to review

Evidence coverage

Prioritization evidence

Off-target risk

Essentiality

Localization

Structure confidence

Binding-site evidence

Cross-references

Sequence

Structure

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