Protein profile

VK055_2879

esterase

Genome: KpATCC43816

Gene: AIK81469.1 yjfP Structure source: Experimental + ColabFold UniProt A0A060VRI4
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Amino acids 233
Annotations 4
Features 7
PDB binders 5
Druggability 0.433

Overview

Basic information about this protein and its source genome.

Accession
VK055_2879
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
AIK81469.1 yjfP
Status
annotated
Amino acids
233
Structure source
Experimental + ColabFold
EC
3.1.1.23
GO
GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. GO:0047372 Catalysis of the reaction: a monoacylglycerol + H2O = a fatty acid + glycerol + H+.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Unknown
ColabFold pLDDT
97.2

Selected Druggability evidence

PDB experimental structure

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.433
Structure 9BD4
Pocket Pocket 2
P2Rank 0.584
Structure 9BD4
Pocket Pocket 1
ColabFold model
FPocket 0.559 · Pocket 4
P2Rank 0.247 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 73 / 4744 genomes with a hit
Normalized 0.015

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

3
  • GO:0008236 Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
  • GO:0006508 The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
  • GO:0047372 Catalysis of the reaction: a monoacylglycerol + H2O = a fatty acid + glycerol + H+.

Sequence Features

Domain/signature hits from InterPro and related databases.

7 records
Show feature table
Start End DB Term Name
2 233 Gene3D G3DSA:3.40.50.1820 alpha/beta hydrolase
2 233 InterPro IPR029058 Alpha/Beta hydrolase fold
46 233 Pfam PF00326 Prolyl oligopeptidase family
46 233 InterPro IPR001375 Peptidase S9, prolyl oligopeptidase, catalytic domain
10 202 PANTHER PTHR22946 UNCHARACTERIZED
14 233 SUPERFAMILY SSF53474 alpha/beta-Hydrolases
14 233 InterPro IPR029058 Alpha/Beta hydrolase fold

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

1 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
PDB 9BD4
X-ray 1.30 Å A,B
100.0% 1-233
PDBe RCSB PDBj File
Viewing
ColabFold VK055_2879
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
19 0.614

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 50.16 0.98
2 7.61 0.402
3 7.34 0.383
4 1.11 0.008

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.

55 records

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
1QW
4KE6
P82597 274.4 Da LogP 2.80 TPSA 66.8 ✓ Ro5 ✓ Clean CCCCCCCCCCCC(=O)OC[C@@H](CO)O
1QX
4KE7
P82597 333.4 Da LogP 5.81 TPSA 95.3 1 viol. Alert CCCCCCCCCCCCOP(=O)(CCCN=[N+]=[N-])O
1QY
4KE8
P82597 361.5 Da LogP 6.59 TPSA 95.3 1 viol. Alert CCCCCCCCCCCCCCO[P@@](=O)(CCCN=[N+]=[N-])O
1R1
4KE9
P82597 389.5 Da LogP 7.37 TPSA 95.3 1 viol. Alert CCCCCCCCCCCCCCCCOP(=O)(CCCN=[N+]=[N-])O
PMS
3RLI
P82597 172.2 Da LogP 1.07 TPSA 54.4 ✓ Ro5 ✓ Clean c1ccc(cc1)CS(=O)(=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.