Protein profile

PA2949

lipase

Genome: NC_002516.2

Gene: PA2949 Structure source: AlphaFold UniProt G3XCU7
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Amino acids 315
Annotations 1
Features 27
PDB binders 8
Druggability 0.897

Overview

Basic information about this protein and its source genome.

Accession
PA2949
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2949
Status
annotated
Amino acids
315
Structure source
AlphaFold
GO
GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
35.955
Human E-value
2.4e-06
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Unknown

Selected Druggability evidence

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 0.897
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 GO

Gene Ontology (GO)

1
  • GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

27 records
Show feature table
Start End DB Term Name
88 103 PRINTS PR00412 Epoxide hydrolase signature
88 103 InterPro IPR000639 Epoxide hydrolase-like
147 160 PRINTS PR00412 Epoxide hydrolase signature
147 160 InterPro IPR000639 Epoxide hydrolase-like
281 303 PRINTS PR00412 Epoxide hydrolase signature
281 303 InterPro IPR000639 Epoxide hydrolase-like
4 19 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
37 304 SUPERFAMILY SSF53474 alpha/beta-Hydrolases
37 304 InterPro IPR029058 Alpha/Beta hydrolase fold
20 28 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
48 306 PANTHER PTHR46438 ALPHA/BETA-HYDROLASES SUPERFAMILY PROTEIN
1 3 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
40 312 Gene3D G3DSA:3.40.50.1820 alpha/beta hydrolase
40 312 InterPro IPR029058 Alpha/Beta hydrolase fold
5 27 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
1 28 Phobius SIGNAL_PEPTIDE Signal peptide region
29 315 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
147 160 PRINTS PR00111 Alpha/beta hydrolase fold signature
147 160 InterPro IPR000073 Alpha/beta hydrolase fold-1
88 103 PRINTS PR00111 Alpha/beta hydrolase fold signature
88 103 InterPro IPR000073 Alpha/beta hydrolase fold-1
133 146 PRINTS PR00111 Alpha/beta hydrolase fold signature
133 146 InterPro IPR000073 Alpha/beta hydrolase fold-1
250 264 PRINTS PR00111 Alpha/beta hydrolase fold signature
250 264 InterPro IPR000073 Alpha/beta hydrolase fold-1
65 298 Pfam PF12697 Alpha/beta hydrolase family
65 298 InterPro IPR000073 Alpha/beta hydrolase fold-1

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

0 + 1

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA2949
AlphaFold — — full sequence — Viewing
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
1 0.897
4 0.881

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.

158 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
ALQ
1IUP
P96965 88.1 Da LogP 0.73 TPSA 37.3 ✓ Ro5 ✓ Clean CC(C)C(=O)O
BEZ
1UKB
P96965 122.1 Da LogP 1.38 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)O
BUA
1UK7
P96965 88.1 Da LogP 0.87 TPSA 37.3 ✓ Ro5 ✓ Clean CCCC(=O)O
FAH
3B12
Q1JU72 78.0 Da LogP 0.04 TPSA 37.3 ✓ Ro5 ✓ Clean C(C(=O)O)F
IVA
1UK9
P96965 102.1 Da LogP 1.12 TPSA 37.3 ✓ Ro5 ✓ Clean CC(C)CC(=O)O
LEA
1UK8
P96965 102.1 Da LogP 1.26 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCC(=O)O
PPI
1UK6
P96965 74.1 Da LogP 0.48 TPSA 37.3 ✓ Ro5 ✓ Clean CCC(=O)O
SMB
1UKA
P96965 102.1 Da LogP 1.12 TPSA 37.3 ✓ Ro5 ✓ Clean CC[C@H](C)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.