3vps

X-ray diffraction
1.9Å resolution

Structure of a novel NAD dependent-NDP-hexosamine 5,6-dehydratase, TunA, involved in tunicamycin biosynthesis

Released:
Entry authors: Wyszynski FJ, Lee SS, Yabe T, Wang H, Gomez-Escribano JP, Bibb MJ, Lee SJ, Davies GJ, Davis BG

Function and Biology Details

Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-122983 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent epimerase/dehydratase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 321 amino acids
Theoretical weight: 35.18 KDa
Source organism: Streptomyces chartreusis NRRL 3882
UniProt:
  • Canonical: E5KJ94 (Residues: 1-321; Coverage: 100%)
Gene name: tunA
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 45.453Å b: 51.061Å c: 67.804Å
α: 98.13° β: 106.65° γ: 94.36°
R-values:
R R work R free
0.188 0.186 0.235