› 5m4o

X-ray diffraction
2.1Å resolution

Crystal structure of hydroquinone 1,2-dioxygenase from Sphingomonas sp. TTNP3 in complex with 4-nitrophenol

Released:
DOI: 10.2210/pdb5m4o/pdb
PDB 5m4o coloured by chain and viewed from the front.
PDB 5m4o coloured by chain and viewed from the side.
PDB 5m4o coloured by chain and viewed from the top.
Source organism: Sphingomonas sp. TTNP3
Primary publication:
The crystal structures of native hydroquinone 1,2-dioxygenase from Sphingomonas sp. TTNP3 and of substrate and inhibitor complexes.
Ferraroni M, Da Vela S, Kolvenbach BA, Corvini PFX, Scozzafava A
Biochim Biophys Acta Proteins Proteom 1865 520-530 (2017)
PMID: 28232026

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hydroquinone dioxygenase small subunit Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 170 amino acids
Theoretical weight: 18.57 KDa
Source organism: Sphingomonas sp. TTNP3
UniProt:
  • Canonical: F8TW82 (Residues: 1-170; Coverage: 100%)
Gene name: hqdA
PnpCD_PnpD_N domain-containing protein Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 341 amino acids
Theoretical weight: 38.24 KDa
Source organism: Sphingomonas sp. TTNP3
UniProt:
  • Canonical: F8TW83 (Residues: 1-341; Coverage: 100%)
Gene name: hqdB
Sequence domains: Hydroquinone 1,2-dioxygenase large subunit N-terminal

Ligands and Environments

2 bound ligands:
Ligand FE 4 x FE
Ligand NPO 4 x NPO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P21
Unit cell:
a: 88.992Å b: 125.982Å c: 92.331Å
α: 90° β: 105.14° γ: 90°
R-values:
R R work R free
0.191 0.188 0.249

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