Protein profile

PA3450

antioxidant protein

Genome: NC_002516.2

Gene: PA3450 Structure source: AlphaFold UniProt Q9HYF6
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Amino acids 212
Annotations 7
Features 17
PDB binders 7
Druggability 0.801

Overview

Basic information about this protein and its source genome.

Accession
PA3450
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3450
Status
annotated
Amino acids
212
Structure source
AlphaFold
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:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O. GO:0051920 Catalysis of the reaction: [protein]-dithol + ROOH = [protein]-disulfide + H2O + ROH. GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell. 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: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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
53.153
Human E-value
8.55e-77
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 0.801
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

7 GO

Gene Ontology (GO)

7
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0004601 Catalysis of the reaction: a reduced substrate + ROOH = an oxidized substrate + ROH + H2O.
  • GO:0051920 Catalysis of the reaction: [protein]-dithol + ROOH = [protein]-disulfide + H2O + ROH.
  • GO:0045454 Any process that maintains the redox environment of a cell or compartment within a cell.
  • 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: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:0098869 Any process carried out at the cellular level that reduces or removes the toxicity superoxide radicals or hydrogen peroxide.

Sequence Features

Domain/signature hits from InterPro and related databases.

17 records
Show feature table
Start End DB Term Name
1 209 PIRSF PIRSF000239 AHPC
1 209 InterPro IPR024706 Peroxiredoxin, AhpC-type
3 210 PANTHER PTHR43503 MCG48959-RELATED
1 145 Gene3D G3DSA:3.40.30.10 Glutaredoxin
5 208 CDD cd03016 PRX_1cys
5 208 InterPro IPR045020 1-Cys peroxiredoxin
146 210 Gene3D G3DSA:3.30.1020.10 Antioxidant, Horf6; Chain A, domain2
3 159 ProSiteProfiles PS51352 Thioredoxin domain profile.
3 159 InterPro IPR013766 Thioredoxin domain
146 210 FunFam G3DSA:3.30.1020.10:FF:000001 1-Cys peroxiredoxin
3 145 FunFam G3DSA:3.40.30.10:FF:000011 Peroxiredoxin PRX1
6 135 Pfam PF00578 AhpC/TSA family
6 135 InterPro IPR000866 Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant
3 209 SUPERFAMILY SSF52833 Thioredoxin-like
3 209 InterPro IPR036249 Thioredoxin-like superfamily
156 191 Pfam PF10417 C-terminal domain of 1-Cys peroxiredoxin
156 191 InterPro IPR019479 Peroxiredoxin, 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 PA3450
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
2 0.801
1 0.254

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.

57 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
BEZ
2V2G
Q1AN22 122.1 Da LogP 1.38 TPSA 37.3 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)O
FL0
7C89
Q9Y9L0 199.0 Da LogP 2.26 TPSA 17.1 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)CBr
FL3
7C8A
Q9Y9L0 170.2 Da LogP 3.04 TPSA 17.1 ✓ Ro5 ✓ Clean CC(=O)c1ccc2ccccc2c1
FLC
3W6G
O58966 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
PE8
4K1F
Q4QF76 370.4 Da LogP -0.91 TPSA 105.1 ✓ Ro5 ✓ Clean C(COCCOCCOCCOCCOCCOCCOCCO)O
PER
3A2V
Q9Y9L0 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.