PDBe 5loc

X-ray diffraction
2.04Å resolution

Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH)

Released:
Source organism: Corynebacterium glutamicum
Entry authors: Dunstan MS, Gahloth D

Function and Biology Details

Reaction catalysed:
Meso-2,6-diaminoheptanedioate + H(2)O + NADP(+) = L-2-amino-6-oxoheptanedioate + NH(3) + NADPH
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Meso-diaminopimelate D-dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 35.06 KDa
Source organism: Corynebacterium glutamicum
Expression system: Escherichia coli
UniProt:
  • Canonical: P04964 (Residues: 2-320; Coverage: 100%)
Gene names: Cgl2617, cg2900, ddh
Sequence domains: Diaminopimelic acid dehydrogenase C-terminal domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3121
Unit cell:
a: 120.53Å b: 120.53Å c: 97.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.207 0.254
Expression system: Escherichia coli