› 6bvs

X-ray diffraction
2.32Å resolution

Crystal structure of 3-hydroxyanthranilate-3,4-dioxygenase I142A from Cupriavidus metallidurans in complex with 4-Cl-3-HAA

Released:
DOI: 10.2210/pdb6bvs/pdb
PDB entry 6bvs coloured by chain, front view.
PDB entry 6bvs coloured by chain, side view.
PDB entry 6bvs coloured by chain, top view.
Source organism: Cupriavidus metallidurans
Primary publication:
Adapting to oxygen: 3-Hydroxyanthrinilate 3,4-dioxygenase employs loop dynamics to accommodate two substrates with disparate polarities.
Yang Y, Liu F, Liu A
J Biol Chem 293 10415-10424 (2018)
PMID: 29784877

Function and Biology Details

Reaction catalysed: 
3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde
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-557344 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxyanthranilate 3,4-dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 195 amino acids
Theoretical weight: 22.55 KDa
Source organism: Cupriavidus metallidurans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q1LCS4 (Residues: 1-174; Coverage: 100%)
Gene names: Rmet_5193, nbaC
Sequence domains: 3-hydroxyanthranilic acid dioxygenase
Structure domains: Jelly Rolls

Ligands and Environments

3 bound ligands:
Ligand 4AA 1 x 4AA
Ligand TRS 1 x TRS
Ligand FE2 2 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6522
Unit cell:
a: 58.306Å b: 58.306Å c: 230.483Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.205 0.255
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Active-site loop variations adjust activity and selectivity of the cumene dioxygenase.
Heinemann et al. (2021)
7 more

1 mention without citation

Adapting to oxygen: 3-Hydroxyanthrinilate 3,4-dioxygenase employs loop dynamics to accommodate two substrates with disparate polarities.
Yang et al. (2018)