Protein profile

PA4615

oxidoreductase

Genome: NC_002516.2

Gene: PA4615 Structure source: AlphaFold UniProt Q9HVH6
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Amino acids 258
Annotations 6
Features 23
PDB binders 2
Druggability 0.664

Overview

Basic information about this protein and its source genome.

Accession
PA4615
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4615
Status
annotated
Amino acids
258
Structure source
AlphaFold
EC
1.18.1.2
GO
GO:0004324 Catalysis of the reaction: 2 reduced [2Fe-2S]-[ferredoxin] + NADP+ + H+ = 2 oxidized [2Fe-2S]-[ferredoxin] + NADPH. GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. GO:0034599 Any process that results in a change in state or activity of a cell (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:0042167 The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. 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 (%)
26.582
Human E-value
4.33e-07
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 0.664
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MTASEEKFTRQTLLDVQPLTPNLFTLRTSRDAGFRFRAGQFARLGVYKPSGSIVWRAYSMVSAPHDEFLDFFSIVVPDGEFTSELSRLREGDQLLVDRQAFGFLTLDRFVDGRDLWLLATGTGVAPFVSILQDFEVWERFESIKLVYSVRESKELAYRELIAGLAEREYLAEHAHKLQFIPVVTREQVPGCLNGRITTLIENGDLERAADLELTPEHSRVMLCGNPQMIEDTRAVLKARGMNLSLTRRPGQVAVENYW

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 5 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

5
  • GO:0004324 Catalysis of the reaction: 2 reduced [2Fe-2S]-[ferredoxin] + NADP+ + H+ = 2 oxidized [2Fe-2S]-[ferredoxin] + NADPH.
  • GO:0000166 Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
  • GO:0034599 Any process that results in a change in state or activity of a cell (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:0042167 The chemical reactions and pathways resulting in the breakdown of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
23 94 Pfam PF00970 Oxidoreductase FAD-binding domain
23 94 InterPro IPR008333 Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain
7 104 SUPERFAMILY SSF63380 Riboflavin synthase domain-like
7 104 InterPro IPR017938 Riboflavin synthase-like beta-barrel
6 107 ProSiteProfiles PS51384 Ferredoxin reductase-type FAD binding domain profile.
6 107 InterPro IPR017927 FAD-binding domain, ferredoxin reductase-type
109 258 SUPERFAMILY SSF52343 Ferredoxin reductase-like, C-terminal NADP-linked domain
109 258 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
103 258 Gene3D G3DSA:3.40.50.80 -
103 258 InterPro IPR039261 Ferredoxin-NADP reductase (FNR), nucleotide-binding domain
103 258 FunFam G3DSA:3.40.50.80:FF:000013 Ferredoxin--NADP(+) reductase
6 258 PANTHER PTHR47878 OXIDOREDUCTASE FAD/NAD(P)-BINDING DOMAIN PROTEIN
117 233 Pfam PF00175 Oxidoreductase NAD-binding domain
117 233 InterPro IPR001433 Oxidoreductase FAD/NAD(P)-binding
12 257 CDD cd06195 FNR1
12 257 InterPro IPR033892 Ferredoxin--NADP reductase, bacteria
1 100 Gene3D G3DSA:2.40.30.10 Translation factors
116 135 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
116 135 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
219 227 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
219 227 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase
56 63 PRINTS PR00371 Flavoprotein pyridine nucleotide cytochrome reductase signature
56 63 InterPro IPR001709 Flavoprotein pyridine nucleotide cytochrome reductase

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 PA4615
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 0.664
4 0.558
3 0.207

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
1JQ4
P22868 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.