4cr7

X-ray diffraction
2.15Å resolution

Crystal structure of the N-acetyl-D-mannosamine dehydrogenase with n-acetylmannosamine

Released:
Source organism: Flavobacterium sp. 141-8
Entry authors: Gil-Ortiz F, Sola-Carvajal A, Garcia-Carmona F, Sanchez-Ferrer A, Rubio V

Function and Biology Details

Reaction catalysed:
N-acyl-D-mannosamine + NAD(+) = N-acyl-D-mannosaminolactone + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acylmannosamine 1-dehydrogenase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 271 amino acids
Theoretical weight: 27.5 KDa
Source organism: Flavobacterium sp. 141-8
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22441 (Residues: 1-271; Coverage: 100%)
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P1
Unit cell:
a: 99.39Å b: 100.12Å c: 111.6Å
α: 67.43° β: 89.75° γ: 72.46°
R-values:
R R work R free
0.202 0.201 0.231
Expression system: Escherichia coli BL21(DE3)