› 6dll

X-ray diffraction
2.2Å resolution

2.2 Angstrom Resolution Crystal Structure of P-Hydroxybenzoate Hydroxylase from Pseudomonas putida in Complex with FAD.

Released:
DOI: 10.2210/pdb6dll/pdb
PDB entry 6dll coloured by chain, front view.
PDB entry 6dll coloured by chain, side view.
PDB entry 6dll coloured by chain, top view.
Source organism: Pseudomonas putida KT2440
Primary publication:
Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases.
Lazar JT, Shuvalova L, Rosas-Lemus M, Kiryukhina O, Satchell KJF, Minasov G
Acta Crystallogr F Struct Biol Commun 75 507-514 (2019)
PMID: 31282871

Function and Biology Details

Reaction catalysed: 
4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183465 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxybenzoate 3-monooxygenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 398 amino acids
Theoretical weight: 44.59 KDa
Source organism: Pseudomonas putida KT2440
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q88H28 (Residues: 1-395; Coverage: 100%)
Gene names: PP_3537, pobA
Sequence domains: FAD binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 4 x FAD
2 bound ligands:
Ligand CL 11 x CL
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 65.041Å b: 152.3Å c: 88.636Å
α: 90° β: 102.43° γ: 90°
R-values:
R R work R free
0.17 0.167 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases.
Lazar et al. (2019)