Protein profile

PA1022

acyl-CoA dehydrogenase

Genome: NC_002516.2

Gene: PA1022 Structure source: AlphaFold UniProt Q9I4V2
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Amino acids 381
Annotations 4
Features 17
PDB binders 2
Druggability 0.824

Overview

Basic information about this protein and its source genome.

Accession
PA1022
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1022
Status
annotated
Amino acids
381
Structure source
AlphaFold
GO
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. GO:0033539 A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
36.275
Human E-value
1.47e-10
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 0.824
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
  • GO:0033539 A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
  • GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
6 117 Gene3D G3DSA:1.10.540.10 -
6 117 InterPro IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
121 231 Gene3D G3DSA:2.40.110.10 -
121 231 InterPro IPR046373 Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
232 381 Gene3D G3DSA:1.20.140.10 -
122 232 FunFam G3DSA:2.40.110.10:FF:000011 Acyl-CoA dehydrogenase FadE34
228 377 Pfam PF00441 Acyl-CoA dehydrogenase, C-terminal domain
228 377 InterPro IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal
9 239 SUPERFAMILY SSF56645 Acyl-CoA dehydrogenase NM domain-like
9 239 InterPro IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
6 381 PANTHER PTHR43292 ACYL-COA DEHYDROGENASE
9 118 Pfam PF02771 Acyl-CoA dehydrogenase, N-terminal domain
9 118 InterPro IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal
122 216 Pfam PF02770 Acyl-CoA dehydrogenase, middle domain
122 216 InterPro IPR006091 Acyl-CoA oxidase/dehydrogenase, middle domain
228 379 SUPERFAMILY SSF47203 Acyl-CoA dehydrogenase C-terminal domain-like
228 379 InterPro IPR036250 Acyl-CoA dehydrogenase-like, C-terminal

3D Structure

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

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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 PA1022
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 0.824

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.

13 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
CAA
1JQI
P15651 851.6 Da LogP -1.36 TPSA 380.7 3 viol. ✓ Clean CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
FDA
4IV6
A0QTW7 787.6 Da LogP -1.75 TPSA 363.3 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…

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.