PDBe 5loa

X-ray diffraction
1.84Å resolution

Crystal structure of the engineered D-Amino Acid Dehydrogenase (DAADH) bound to NADP+

Released:
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: 319 amino acids
Theoretical weight: 35 KDa
Source organism: Corynebacterium glutamicum ATCC 13032
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


Cofactor: Ligand NAP 2 x NAP
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 75.02Å b: 64.58Å c: 82.06Å
α: 90° β: 106.89° γ: 90°
R-values:
R R work R free
0.173 0.172 0.206
Expression system: Escherichia coli