Protein profile

PA0247

4-hydroxybenzoate 3-monooxygenase

Genome: NC_002516.2

Gene: pobA PA0247 Structure source: Experimental + AlphaFold UniProt P20586
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Amino acids 394
Annotations 8
Features 16
PDB binders 11
Druggability 0.734

Overview

Basic information about this protein and its source genome.

Accession
PA0247
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
pobA PA0247
Status
annotated
Amino acids
394
Structure source
Experimental + AlphaFold
EC
1.14.13.2
GO
GO:0106356 Catalysis of the reaction: 4-hydroxybenzoate + H+ + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP+. GO:0018659 Catalysis of the reaction: 4-hydroxybenzoate + NADPH + H+ + O2 = protocatechuate + NADP+ + H2O. GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. 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: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:0043640 The chemical reactions and pathways resulting in the breakdown of benzoate, by its hydroxylation to cis-1,2-dihydroxybenzoate followed by dehydrogenation to catechol.

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 0.734
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0106356 Catalysis of the reaction: 4-hydroxybenzoate + H+ + NADPH + O2 = 3,4-dihydroxybenzoate + H2O + NADP+.
  • GO:0018659 Catalysis of the reaction: 4-hydroxybenzoate + NADPH + H+ + O2 = protocatechuate + NADP+ + H2O.
  • GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • 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: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:0043640 The chemical reactions and pathways resulting in the breakdown of benzoate, by its hydroxylation to cis-1,2-dihydroxybenzoate followed by dehydrogenation to catechol.
  • GO:0043639 The chemical reactions and pathways resulting in the breakdown of benzoate, the anion of benzoic acid (benzenecarboxylic acid), a fungistatic compound widely used as a food preservative; it is conjugated to glycine in the liver and excreted as hippuric acid.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
175 275 SUPERFAMILY SSF54373 FAD-linked reductases, C-terminal domain
2 351 Gene3D G3DSA:3.50.50.60 -
2 351 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
1 389 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
1 389 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
3 328 PANTHER PTHR43476 3-(3-HYDROXY-PHENYL)PROPIONATE/3-HYDROXYCINNAMIC ACID HYDROXYLASE
2 343 Pfam PF01494 FAD binding domain
2 343 InterPro IPR002938 FAD-binding domain
4 26 PRINTS PR00420 Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
278 293 PRINTS PR00420 Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
310 328 PRINTS PR00420 Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
151 166 PRINTS PR00420 Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
293 309 PRINTS PR00420 Aromatic-ring hydroxylase (flavoprotein monooxygenase) signature
73 388 Gene3D G3DSA:3.30.9.10 -
1 390 NCBIfam TIGR02360 4-hydroxybenzoate 3-monooxygenase
1 390 InterPro IPR012733 4-hydroxybenzoate 3-monooxygenase

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

20 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
PDB 6JU1
X-ray 1.60 Å A
100.0% 1-394
PDBe RCSB PDBj File
Viewing
PDB 1K0I
X-ray 1.80 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1DOB
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1DOC
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1IUT
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1IUU
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1IUW
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1IUX
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1K0L
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1YKJ
X-ray 2.00 Å A,B
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1DOD
X-ray 2.10 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1PXC
X-ray 2.10 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1D7L
X-ray 2.20 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1IUS
X-ray 2.20 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1K0J
X-ray 2.20 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1DOE
X-ray 2.30 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1PXA
X-ray 2.30 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1PXB
X-ray 2.30 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 1IUV
X-ray 2.50 Å A
100.0% 1-394
PDBe RCSB PDBj File
Loaded
PDB 8Y2S
X-ray 2.00 Å A
100.0% 1-394
PDBe RCSB PDBj File
Metadata only
AlphaFold PA0247
AlphaFold — — full sequence — Loaded
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 0.734

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 40.09 0.963
2 2.55 0.072
3 2.54 0.071
4 2.24 0.055
5 0.86 0.003

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.

62 records

Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.

Show only:
Ligand Source crystal MW · LogP · TPSA Lipinski PAINS SMILES
PSL
1YKJ 2.00 Å Open crystal
176.1 Da LogP -2.08 TPSA 123.6 ✓ Ro5 ✓ Clean [O-]S(=O)(=O)OS(=O)(=O)[O-]
RFL
1D7L 2.20 Å Open crystal
814.6 Da LogP -2.67 TPSA 366.2 3 viol. ✓ Clean Cc1cc2c(cc1N(C)C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]…

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.