Protein profile

PA0883

acyl-CoA lyase subunit beta

Genome: NC_002516.2

Gene: PA0883 Structure source: Experimental + AlphaFold UniProt Q9I562
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Amino acids 275
Annotations 4
Features 10
PDB binders 8
Druggability 0.742

Overview

Basic information about this protein and its source genome.

Accession
PA0883
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0883
Status
annotated
Amino acids
275
Structure source
Experimental + AlphaFold
GO
GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. GO:0000287 Binding to a magnesium (Mg) ion. GO:0006107 The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle. 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 (%)
32.979
Human E-value
2.83e-11
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

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 0.742
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MNRQIVRSALFVPATRPERIPKALASGADRVIVDLEDAVEEGLKVEARANLRRFLVDTPEARVLVRINAAEHPGHADDLALCRDHAGVIGLLLPKVESAAQVRHAAVASGKPVWPIVESARGLAALGEIAAAAGVERLSFGSLDLALDLDLNSGSNAAEQILGHARYALLLQTRLAGLAPPLDGVYPAIQNRAGLVEAVRFARDMGFGGLLCIHPSQVEPIHQTLMPSPAELEWARRVAEAGASGAGVFVVDGEMVDAPVLGRARRLLERAGEGG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0016829 Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0006107 The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.
  • 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.

10 records
Show feature table
Start End DB Term Name
4 272 PANTHER PTHR32308 LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED
1 275 Gene3D G3DSA:3.20.20.60 -
1 275 InterPro IPR040442 Pyruvate kinase-like domain superfamily
1 275 PIRSF PIRSF015582 Cit_lyase_B
1 275 InterPro IPR011206 Citrate lyase beta subunit-like
1 275 FunFam G3DSA:3.20.20.60:FF:000059 Acyl-CoA lyase subunit beta
4 227 SUPERFAMILY SSF51621 Phosphoenolpyruvate/pyruvate domain
4 227 InterPro IPR015813 Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
7 215 Pfam PF03328 HpcH/HpaI aldolase/citrate lyase family
7 215 InterPro IPR005000 HpcH/HpaI aldolase/citrate lyase domain

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

3 + 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 9NZB
X-ray 1.85 Å A,B,C,D,E,F
100.0% 1-275
PDBe RCSB PDBj File
Viewing
PDB 8KHL
X-ray 2.40 Å A,B,C
100.0% 1-275
PDBe RCSB PDBj File
Loaded
PDB 8WCO
X-ray 2.60 Å A,B,C
100.0% 1-275
PDBe RCSB PDBj File
Loaded
AlphaFold PA0883
AlphaFold — — 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
1 0.742
3 0.208

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 11.49 0.613
2 7.24 0.377

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.

58 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
1VU
4L9Y
Q3J5L6 823.6 Da LogP -0.93 TPSA 363.6 3 viol. ✓ Clean CCC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(=O)(O…
AAE
6AS5
P9WPE1 102.1 Da LogP 0.05 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=O)CC(=O)O
CQM
6AQ4
P9WPE1 897.6 Da LogP -2.11 TPSA 421.2 3 viol. ✓ Clean C[C@](CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)COP(…
CSO
6AQ4
P9WPE1 137.2 Da LogP -0.40 TPSA 83.5 ✓ Ro5 ✓ Clean C([C@@H](C(=O)O)N)SO
GLV
4L9Y
Q3J5L6 74.0 Da LogP -0.73 TPSA 54.4 ✓ Ro5 ✓ Clean C(=O)C(=O)O
OAA
1Z6K
P9WPE1 131.1 Da LogP -2.22 TPSA 94.5 ✓ Ro5 ✓ Clean C(C(=O)C(=O)O)C(=O)[O-]
OXL
4L9Z
Q3J5L6 88.0 Da LogP -3.51 TPSA 80.3 ✓ Ro5 ✓ Clean C(=O)(C(=O)[O-])[O-]
PYR
6AQ4
P9WPE1 88.1 Da LogP -0.34 TPSA 54.4 ✓ Ro5 ✓ Clean CC(=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.