Protein profile

PA0139

alkyl hydroperoxide reductase

Genome: NC_002516.2

Gene: PA0139 ahpC Structure source: AlphaFold UniProt Q9I6Z3
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Amino acids 187
Annotations 10
Features 16
PDB binders 6
Druggability 0.936

Overview

Basic information about this protein and its source genome.

Accession
PA0139
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA0139 ahpC
Status
annotated
Amino acids
187
Structure source
AlphaFold
EC
1.11.1.26
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0102039 Catalysis of the reaction: a hydroperoxide + H+ + NADH = an alcohol + H2O + NAD+. GO:0008379 Catalysis of the reaction: [thioredoxin]-dithiol + H2O2 = [thioredoxin]-disulfide + H2O. GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell. GO:0042744 The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2). GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
42.458
Human E-value
3.26e-41
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 0.936
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0102039 Catalysis of the reaction: a hydroperoxide + H+ + NADH = an alcohol + H2O + NAD+.
  • GO:0008379 Catalysis of the reaction: [thioredoxin]-dithiol + H2O2 = [thioredoxin]-disulfide + H2O.
  • GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
  • GO:0042744 The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2).
  • GO:0006979 Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.
  • GO:0016209 Inhibition of the reactions brought about by dioxygen (O2) or peroxides. Usually the antioxidant is effective because it can itself be more easily oxidized than the substance protected. The term is often applied to components that can trap free radicals, thereby breaking the chain reaction that normally leads to extensive biological damage.
  • GO:0051920 Catalysis of the reaction: [protein]-dithol + ROOH = [protein]-disulfide + H2O + ROH.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
1 185 Gene3D G3DSA:3.40.30.10 Glutaredoxin
3 180 PANTHER PTHR10681 THIOREDOXIN PEROXIDASE
1 187 FunFam G3DSA:3.40.30.10:FF:000002 Alkyl hydroperoxide reductase C
1 187 NCBIfam TIGR03137 alkyl hydroperoxide reductase subunit C (peroxiredoxin)
1 187 InterPro IPR017559 Alkyl hydroperoxide reductase subunit C
4 132 Pfam PF00578 AhpC/TSA family
4 132 InterPro IPR000866 Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant
155 182 Pfam PF10417 C-terminal domain of 1-Cys peroxiredoxin
155 182 InterPro IPR019479 Peroxiredoxin, C-terminal
1 187 PIRSF PIRSF000239 AHPC
1 187 InterPro IPR024706 Peroxiredoxin, AhpC-type
4 173 CDD cd03015 PRX_Typ2cys
2 157 ProSiteProfiles PS51352 Thioredoxin domain profile.
2 157 InterPro IPR013766 Thioredoxin domain
1 186 SUPERFAMILY SSF52833 Thioredoxin-like
1 186 InterPro IPR036249 Thioredoxin-like superfamily

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 PA0139
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
5 0.936
2 0.496
1 0.293

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.

31 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
COM
4RQX
Q13162 142.2 Da LogP -0.20 TPSA 54.4 ✓ Ro5 ✓ Clean C(CS(=O)(=O)O)S
DTU
3SBC
P34760 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@H]([C@H](CS)O)O)S
DTV
3SBC
P34760 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@H]([C@@H](CS)O)O)S
NH4
1WE0
K0J4Q8 18.0 Da LogP 0.38 TPSA 36.5 ✓ Ro5 ✓ Clean [NH4+]
PER
3TKS
Q13162 32.0 Da LogP -2.38 TPSA 46.1 ✓ Ro5 ✓ Clean [O-][O-]
QDO
4KW6
J7HJM3 348.0 Da LogP 1.90 TPSA 53.9 ✓ Ro5 Alert c1ccc2c(c1)[n+](c(c([n+]2[O-])CBr)CBr)[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.