Protein profile

PA2325

hypothetical protein

Genome: NC_002516.2

Gene: PA2325 Structure source: AlphaFold UniProt Q9I1F3
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Amino acids 411
Annotations 6
Features 17
PDB binders 5
Druggability 0.793

Overview

Basic information about this protein and its source genome.

Accession
PA2325
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2325
Status
annotated
Amino acids
411
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0003995 Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. 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. GO:0016712 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
22.701
Human E-value
2.22e-08
Gut microbiome off-target
hit
Essential (DEG)
Y
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 0.793
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0003995 Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
  • 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.
  • GO:0016712 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from reduced flavin or flavoprotein and one other donor, and one atom of oxygen is incorporated into one donor.
  • 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: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.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
254 386 Pfam PF08028 Acyl-CoA dehydrogenase, C-terminal domain
254 386 InterPro IPR013107 Acyl-CoA dehydrogenase, C-terminal domain
136 234 Gene3D G3DSA:2.40.110.10 -
136 234 InterPro IPR046373 Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
18 133 Gene3D G3DSA:1.10.540.10 -
18 133 InterPro IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
43 386 PANTHER PTHR48083 MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED
33 235 SUPERFAMILY SSF56645 Acyl-CoA dehydrogenase NM domain-like
33 235 InterPro IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
235 410 Gene3D G3DSA:1.20.140.10 -
237 410 SUPERFAMILY SSF47203 Acyl-CoA dehydrogenase C-terminal domain-like
237 410 InterPro IPR036250 Acyl-CoA dehydrogenase-like, C-terminal
21 411 NCBIfam TIGR04022 SfnB family sulfur acquisition oxidoreductase
21 411 InterPro IPR023922 Sulphate-starvation-induced SfnB
14 406 PIRSF PIRSF016578 PIGM
42 126 Pfam PF02771 Acyl-CoA dehydrogenase, N-terminal domain
42 126 InterPro IPR013786 Acyl-CoA dehydrogenase/oxidase, N-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 PA2325
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 0.793
2 0.418

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
83R
5XDE
Q9LBX2 184.3 Da LogP 4.05 TPSA 0.0 ✓ Ro5 ✓ Clean c1ccc2c(c1)c3ccccc3s2
83U
5XDG
Q9LBX2 200.3 Da LogP 2.83 TPSA 17.1 ✓ Ro5 ✓ Clean c1ccc2c(c1)-c3ccccc3S2=O
COS
5OL2
A0A031WJ47 799.6 Da LogP -1.02 TPSA 346.6 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…
FDA
3PFD
G7CNE7 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…
IND
5LVW
I7IIA9 117.2 Da LogP 2.17 TPSA 15.8 ✓ Ro5 ✓ Clean c1ccc2c(c1)cc[nH]2

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.