3vsi

X-ray diffraction
2.5Å resolution

Crystal structure of native 1,6-APD (2-Animophenol-1,6-dioxygenase) complex with 4-Nitrocatechol

Released:
Source organism: Comamonas testosteroni CNB-1
Primary publication:
Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor.
Acta Crystallogr D Biol Crystallogr 69 32-43 (2013)
PMID: 23275161

Function and Biology Details

Reactions catalysed:
Protocatechuate + O(2) = 4-carboxy-2-hydroxymuconate semialdehyde
2-aminophenol + O(2) = 2-aminomuconate 6-semialdehyde
2-amino-5-chlorophenol + O(2) = 2-amino-5-chloromuconate 6-semialdehyde
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-179801 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
2-aminophenol 1,6-dioxygenase subunit alpha Chains: A, C
Molecule details ›
Chains: A, C
Length: 271 amino acids
Theoretical weight: 29.3 KDa
Source organism: Comamonas testosteroni CNB-1
UniProt:
  • Canonical: Q6J1Z5 (Residues: 1-271; Coverage: 100%)
Gene names: amnA, cnbCa
Sequence domains: Catalytic LigB subunit of aromatic ring-opening dioxygenase
Structure domains: LigB-like
2-aminophenol 1,6-dioxygenase subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 312 amino acids
Theoretical weight: 35.08 KDa
Source organism: Comamonas testosteroni CNB-1
UniProt:
  • Canonical: Q6J1Z6 (Residues: 1-312; Coverage: 100%)
Gene names: amnB, cnbCb
Sequence domains: Catalytic LigB subunit of aromatic ring-opening dioxygenase
Structure domains: LigB-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 272.73Å b: 48.26Å c: 108.12Å
α: 90° β: 109.61° γ: 90°
R-values:
R R work R free
0.208 0.204 0.27