Protein profile

PA1538

flavin-containing monooxygenase

Genome: NC_002516.2

Gene: PA1538 Structure source: AlphaFold UniProt Q9I3H5
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Amino acids 527
Annotations 6
Features 12
PDB binders 7
Druggability 0.81

Overview

Basic information about this protein and its source genome.

Accession
PA1538
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1538
Status
annotated
Amino acids
527
Structure source
AlphaFold
EC
1.14.13.-
GO
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:0004497 Catalysis of the incorporation of one atom of molecular oxygen (O2) into the substrate and the reduction of the other atom of O2 to water. GO:0004499 Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O. GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. GO:0016709 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
26.432
Human E-value
3.32e-09
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 0.81
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

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: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:0004497 Catalysis of the incorporation of one atom of molecular oxygen (O2) into the substrate and the reduction of the other atom of O2 to water.
  • GO:0004499 Catalysis of the reaction: N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
  • GO:0050661 Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH.
  • GO:0016709 Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor.

Sequence Features

Domain/signature hits from InterPro and related databases.

12 records
Show feature table
Start End DB Term Name
19 259 Gene3D G3DSA:3.50.50.60 -
19 259 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
323 508 Gene3D G3DSA:3.50.50.60 -
323 508 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
324 510 FunFam G3DSA:3.50.50.60:FF:000266 Baeyer-Villiger monooxygenase
298 500 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
298 500 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
16 509 PANTHER PTHR42877 -
24 251 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
24 251 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
27 229 Pfam PF00743 Flavin-binding monooxygenase-like
27 229 InterPro IPR020946 Flavin monooxygenase-like

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 PA1538
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 0.646

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
6NA
6GQI
A0A1L1QK40 116.2 Da LogP 1.65 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCC(=O)O
CYH
3UCL
C0STX7 98.1 Da LogP 1.52 TPSA 17.1 ✓ Ro5 ✓ Clean C1CCC(=O)CC1
MMZ
5GSN
A3SLM3 114.2 Da LogP 1.08 TPSA 20.7 ✓ Ro5 ✓ Clean CN1C=CNC1=S
N01
4C74
Q47PU3 739.4 Da LogP -4.32 TPSA 350.1 2 viol. ✓ Clean CC(=O)c1ccc[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2…
NA7
5M0Z
A0A1L1QK39 623.3 Da LogP -2.48 TPSA 317.8 3 viol. ✓ Clean c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)…
NCA
5M10
A0A1L1QK40 122.1 Da LogP 0.18 TPSA 56.0 ✓ Ro5 ✓ Clean c1cc(cnc1)C(=O)N
PTD
4RG4
C0STX7 100.1 Da LogP 0.55 TPSA 34.1 ✓ Ro5 ✓ Clean C(CC=O)CC=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.