KpATCC43816 Protein target profile

alpha/beta hydrolase fold family protein

Accession: VK055_0706

Gene: AIK79329.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism Not in network UniProt A0A060VHX3
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Length 217
Pocket druggability (P2Rank · AlphaFold DB model) 0.81
Direct ligand evidence 0 157 total records
Functional annotation 1 EC 2 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

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 0.81. Structure available AlphaFold DB model + ColabFold model Ligand evidence via structure/bioactivity 7 structural and 100 bioactivity records.

Risks to review

Microbiome similarity 3 of 4744 screened genomes (0.1%) have a significant similarity hit. This target also has a predicted binding pocket (P2Rank 0.81) — check the ligand evidence before deprioritizing on off-target risk alone. Mixed conservation Core/accessory calls are not fully concordant. Best pocket may be a modeling artifact FPocket selected-pocket score 0.91, but this pocket's geometry is unusually large/diffuse compared to this protein's other predicted pockets — may reflect a low-confidence or disordered model region rather than a real cavity.

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
0.1% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

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

Structure confidence

ColabFold pLDDT
95.35 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.81
Structure A0A060VHX3
Pocket Pocket 1
Druggability (FPocket) 0.912
Structure A0A060VHX3
Pocket Pocket 1
ColabFold model
P2Rank 0.959 · Pocket 1
FPocket 0.861 · Pocket 10
Core conservation Accessory gene
Roary accessory
CoreCruncher accessory
Gut microbiome 3 / 4744 genomes with a hit
Prevalence 0.1%

Metabolic context

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

This protein is not associated with the imported metabolic network for this genome.

Browse the genome's metabolic network

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MLNEMLWHEFETYLPSNCIVHHAAVTEGRTIHDVVQHLITLLPEKFSLIGFSMGGYIARQLAAEFPERVESLVLIASSLREDTPLEAEAKRKSVQSLSPTTFKGLSRHAIARSLHPLNTSNQDMISAIQKMGCSLGFEAFITQSSLSRQGIPSATIRCPTLVIASEDDAIRSMKEAEELVEAIPYASLRIILDCGHMIPLEQPRELARIIVEWIPAT

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 2 GO

Subcellular localization

Localization
Cytoplasmic

Enzyme Commission (EC)

1

Gene Ontology (GO)

2
  • GO:0016787 Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
  • GO:0016740 Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

13 records
Show feature table
Start End DB Term Name
28 214 SUPERFAMILY SSF53474 alpha/beta-Hydrolases
28 214 InterPro IPR029058 Alpha/Beta hydrolase fold
33 214 PANTHER PTHR43798 MONOACYLGLYCEROL LIPASE
19 216 Gene3D G3DSA:3.40.50.1820 alpha/beta hydrolase
19 216 InterPro IPR029058 Alpha/Beta hydrolase fold
40 202 Pfam PF00561 alpha/beta hydrolase fold
40 202 InterPro IPR000073 Alpha/beta hydrolase fold-1
160 174 PRINTS PR00111 Alpha/beta hydrolase fold signature
160 174 InterPro IPR000073 Alpha/beta hydrolase fold-1
62 75 PRINTS PR00111 Alpha/beta hydrolase fold signature
62 75 InterPro IPR000073 Alpha/beta hydrolase fold-1
48 61 PRINTS PR00111 Alpha/beta hydrolase fold signature
48 61 InterPro IPR000073 Alpha/beta hydrolase fold-1

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.

Download VMD script Full viewer

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Drag to rotate — click the view, then scroll to zoom.

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 · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1
0.81
Likely same site as FPocket 1 1.9 Å 19 shared residues 86% of smaller site
Show in viewer
Surrounding area
Pocket 2 P2Rank #2
0.003
Show in viewer
Surrounding area

Binding pockets · FPocket

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

Pocket 1 FPocket #1
0.912 Unusual size
Likely same site as P2Rank 1 1.9 Å 19 shared residues 86% of smaller site
Show in viewer
Surrounding area
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_A0A060VHX3
AlphaFold DB — — full sequence — Viewing
ColabFold VK055_0706
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.

157 records
Chemistry signal

Structural and bioactivity evidence are both available for this target.

Direct evidence 0 same-protein records
Transferred evidence 107 records from similar proteins
Structural ligands 7 0 loaded crystals
Measured bioactivity 100 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
6OR PDB via homolog 243.1 Da · LogP 1.95 · TPSA 74.6 Open detail RCSB PDB
6OT PDB via homolog Detail RCSB PDB
FGZ PDB via homolog Detail RCSB PDB
HPK PDB via homolog Detail RCSB PDB
KEK PDB via homolog Detail RCSB PDB

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.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
6OR RCSB PDB
5JZ9
P9WNH5 243.1 Da LogP 1.95 TPSA 74.6 ✓ Ro5 ✓ Clean c1c(cc(c(c1Cl)O)Cl)S(=O)(=O)O
6OT RCSB PDB
5JZB
P9WNH5 226.1 Da LogP 1.64 TPSA 60.2 ✓ Ro5 ✓ Clean c1c(cc(cc1Cl)Cl)S(=O)(=O)N
FGZ RCSB PDB
5JZS
P9WNH5 207.0 Da LogP 2.40 TPSA 57.5 ✓ Ro5 ✓ Clean c1c(cc(c(c1Cl)O)Cl)C(=O)O
HPK RCSB PDB
2WUG
P9WNH5 217.2 Da LogP 0.13 TPSA 74.3 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)C\C=C\C(=O)C(=O)[O-]
KEK RCSB PDB
2WUE
P9WNH5 293.7 Da LogP 1.35 TPSA 74.3 ✓ Ro5 ✓ Clean C[C@H](\C=C\C(=O)C(=O)[O-])C(=O)CCc1ccccc1Cl
KEM RCSB PDB
2WUF
P9WNH5 349.4 Da LogP 0.60 TPSA 111.6 ✓ Ro5 ✓ Clean C[C@H](\C=C\C(=O)C(=O)[O-])C(=O)CC[C@@H]1[C@H]2…
MLT RCSB PDB
4UHE
A0A0M3KKY6 134.1 Da LogP -1.09 TPSA 94.8 ✓ Ro5 ✓ Clean C([C@H](C(=O)O)O)C(=O)O

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.

Cross-references

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

Sequence

UniProt A0A060VHX3

Chemistry

ChEMBL CHEMBL3263577 ChEMBL CHEMBL3263579 ChEMBL CHEMBL3263582 ChEMBL CHEMBL5274434 ChEMBL CHEMBL3895863 ChEMBL CHEMBL3906477 ChEMBL CHEMBL4279328 ChEMBL CHEMBL4279884 ChEMBL CHEMBL4287766 ChEMBL CHEMBL4581240 ChEMBL CHEMBL4289572 ChEMBL CHEMBL4284689 ChEMBL CHEMBL3318603 ChEMBL CHEMBL3318604 ChEMBL CHEMBL3318612 ChEMBL CHEMBL4277989 ChEMBL CHEMBL4281842 ChEMBL CHEMBL4294845 ChEMBL CHEMBL3964338 ChEMBL CHEMBL3970032 ChEMBL CHEMBL4291201 ChEMBL CHEMBL4281906 ChEMBL CHEMBL2144065 ChEMBL CHEMBL3897587 ChEMBL CHEMBL3931744 ChEMBL CHEMBL3974512 ChEMBL CHEMBL3613671 ChEMBL CHEMBL5284566 ChEMBL CHEMBL3913807 ChEMBL CHEMBL606201 ChEMBL CHEMBL5740302 ChEMBL CHEMBL5743322 ChEMBL CHEMBL5753028 ChEMBL CHEMBL5756639 ChEMBL CHEMBL5758154 ChEMBL CHEMBL5768449 ChEMBL CHEMBL5772306 ChEMBL CHEMBL5782109 ChEMBL CHEMBL5788039 ChEMBL CHEMBL5821624 ChEMBL CHEMBL5825092 ChEMBL CHEMBL5832448 ChEMBL CHEMBL5851382 ChEMBL CHEMBL5855121 ChEMBL CHEMBL5859637 ChEMBL CHEMBL5860073 ChEMBL CHEMBL5864851 ChEMBL CHEMBL5874842 ChEMBL CHEMBL5893433 ChEMBL CHEMBL5901346 ChEMBL CHEMBL5913237 ChEMBL CHEMBL5937515 ChEMBL CHEMBL5945082 ChEMBL CHEMBL5949603 ChEMBL CHEMBL5950082 ChEMBL CHEMBL5962041 ChEMBL CHEMBL5962440 ChEMBL CHEMBL5965548 ChEMBL CHEMBL5983321 ChEMBL CHEMBL5985697 ChEMBL CHEMBL5996161 ChEMBL CHEMBL5998219 ChEMBL CHEMBL6009697 ChEMBL CHEMBL6015117 ChEMBL CHEMBL6022031 ChEMBL CHEMBL6029886 ChEMBL CHEMBL6035930 ChEMBL CHEMBL6040703 ChEMBL CHEMBL6052770 ChEMBL CHEMBL3318590 ChEMBL CHEMBL600429 ChEMBL CHEMBL4068554 ChEMBL CHEMBL3613162 ChEMBL CHEMBL4462665 ChEMBL CHEMBL4469632 ChEMBL CHEMBL4289712 ChEMBL CHEMBL4436074 ChEMBL CHEMBL3922787 ChEMBL CHEMBL3613161 ChEMBL CHEMBL3979183 ChEMBL CHEMBL591688 ChEMBL CHEMBL597515 ChEMBL CHEMBL3897762 ChEMBL CHEMBL3912754 ChEMBL CHEMBL3941507 ChEMBL CHEMBL4288486 ChEMBL CHEMBL3894067 ChEMBL CHEMBL599731 ChEMBL CHEMBL604948 ChEMBL CHEMBL3910417 ChEMBL CHEMBL4584757 ChEMBL CHEMBL3916842 ChEMBL CHEMBL3921538 ChEMBL CHEMBL3983619 ChEMBL CHEMBL3318611 ChEMBL CHEMBL601243 ChEMBL CHEMBL601244 ChEMBL CHEMBL3903742 ChEMBL CHEMBL3904310 ChEMBL CHEMBL3945728