Protein profile

PA3498

oxidoreductase

Genome: NC_002516.2

Gene: PA3498 Structure source: AlphaFold UniProt Q9HYB1
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Amino acids 318
Annotations 4
Features 32
PDB binders 2
Druggability 0.649

Overview

Basic information about this protein and its source genome.

Accession
PA3498
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3498
Status
annotated
Amino acids
318
Structure source
AlphaFold
GO
GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. GO:0046872 Binding to a metal ion. 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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.649
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MTHDNRLAAFVHTLRFEAQGILGVELRPQGDQVFPPFSAGAHIDLHLPNGLVRSYSLLNSPEDCGRYVLGILRDRGSRGGSAFVHDSLRVGMQLQISRPRNLFPLEENAAHSVLVAGGIGVTPIYCMFNRLRALGRSVELLYCARSRQEAAFVEELAASDAAIQLHFDDEKGGPMDLGAFLGARASTAHFYCCGPTPMIDAFETHCERLGHPHVHIERFAAAPQAPAAPQGSYEVRLARSGTSIEVPSGKSLLDALLEAGVAVDCSCREGVCGSCETRVLEGEPEHRDGVLTKAEKIANQTMMVCVSGCKGSRLVLDL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

4 GO

Gene Ontology (GO)

4
  • GO:0051537 Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
  • GO:0046872 Binding to a metal ion.
  • 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:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.

Sequence Features

Domain/signature hits from InterPro and related databases.

32 records
Show feature table
Start End DB Term Name
8 317 PANTHER PTHR47354 NADH OXIDOREDUCTASE HCR
233 318 ProSiteProfiles PS51085 2Fe-2S ferredoxin-type iron-sulfur binding domain profile.
233 318 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
15 219 CDD cd06185 PDR_like
41 53 PRINTS PR00409 Phthalate dioxygenase reductase family signature
77 91 PRINTS PR00409 Phthalate dioxygenase reductase family signature
138 147 PRINTS PR00409 Phthalate dioxygenase reductase family signature
189 197 PRINTS PR00409 Phthalate dioxygenase reductase family signature
113 132 PRINTS PR00409 Phthalate dioxygenase reductase family signature
31 41 PRINTS PR00409 Phthalate dioxygenase reductase family signature
91 105 PRINTS PR00409 Phthalate dioxygenase reductase family signature
53 67 PRINTS PR00409 Phthalate dioxygenase reductase family signature
99 223 SUPERFAMILY SSF52343 Ferredoxin reductase-like, C-terminal NADP-linked domain
99 223 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
239 307 CDD cd00207 fer2
239 307 InterPro IPR001041 2Fe-2S ferredoxin-type iron-sulfur binding domain
4 106 ProSiteProfiles PS51384 Ferredoxin reductase-type FAD binding domain profile.
4 106 InterPro IPR017927 FAD-binding domain, ferredoxin reductase-type
103 219 Gene3D G3DSA:3.40.50.80 -
103 219 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
2 102 Gene3D G3DSA:2.40.30.10 Translation factors
114 202 Pfam PF00175 Oxidoreductase NAD-binding domain
114 202 InterPro IPR001433 Oxidoreductase FAD/NAD(P)-binding
4 101 SUPERFAMILY SSF63380 Riboflavin synthase domain-like
4 101 InterPro IPR017938 Riboflavin synthase-like beta-barrel
267 275 ProSitePatterns PS00197 2Fe-2S ferredoxin-type iron-sulfur binding region signature.
267 275 InterPro IPR006058 2Fe-2S ferredoxin, iron-sulphur binding site
239 307 Pfam PF00111 2Fe-2S iron-sulfur cluster binding domain
212 316 SUPERFAMILY SSF54292 2Fe-2S ferredoxin-like
212 316 InterPro IPR036010 2Fe-2S ferredoxin-like superfamily
223 318 Gene3D G3DSA:3.10.20.30 -
223 318 InterPro IPR012675 Beta-grasp domain 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 PA3498
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
4 0.649

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
FDA
1TVC
P22868 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…
FES
6LAA
A0A0K6ITW2 175.8 Da LogP 1.29 TPSA 0.0 ✓ Ro5 ✓ Clean S1[Fe]S[Fe]1

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.