› 5k8n

X-ray diffraction
3.22Å resolution

5NAA-bound 5-nitroanthranilate aminohydrolase

Released:
DOI: 10.2210/pdb5k8n/pdb
PDB 5k8n coloured by chain and viewed from the front.
PDB 5k8n coloured by chain and viewed from the side.
PDB 5k8n coloured by chain and viewed from the top.
Source organism: Bradyrhizobium sp.
Primary publication:
Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.
Kalyoncu S, Heaner DP, Kurt Z, Bethel CM, Ukachukwu CU, Chakravarthy S, Spain JC, Lieberman RL
Nat. Chem. Biol. (2016)
PMID: 27694799

Function and Biology Details

Reaction catalysed: 
5-nitroanthranilate + H(2)O = 5-nitrosalicylate + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-nitroanthranilic acid aminohydrolase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 425 amino acids
Theoretical weight: 46.4 KDa
Source organism: Bradyrhizobium sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: D3WZ85 (Residues: 1-425; Coverage: 100%)
Gene name: naaA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 6R6 8 x 6R6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 186.463Å b: 248.875Å c: 249.284Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.217
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

A triphenylamine-functionalized luminescent sensor for efficient p-nitroaniline detection.
Ji et al. (2018)
2 more

1 mention without citation

Enzymatic hydrolysis by transition-metal-dependent nucleophilic aromatic substitution.
Kalyoncu et al. (2016)