› 4cr6

X-ray diffraction
1.9Å resolution

Crystal structure of the N-acetyl-D-mannosamine dehydrogenase without substrates

Released:
DOI: 10.2210/pdb4cr6/pdb
PDB entry 4cr6 coloured by chain, front view.
PDB entry 4cr6 coloured by chain, side view.
PDB entry 4cr6 coloured by chain, top view.
Source organism: Flavobacterium sp. 141-8
Primary publication:
Crystal structures and functional studies clarify substrate selectivity and catalytic residues for the unique orphan enzyme N-acetyl-D-mannosamine dehydrogenase.
Sola-Carvajal A, Gil-Ortiz F, García-Carmona F, Rubio V, Sánchez-Ferrer Á
Biochem J 462 499-511 (2014)
PMID: 24969681

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-540155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acylmannosamine 1-dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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

1 bound ligand:
Ligand MAN 2 x MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P1
Unit cell:
a: 59.255Å b: 59.062Å c: 74.206Å
α: 81.13° β: 73.29° γ: 79.25°
R-values:
R R work R free
0.21 0.209 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Crystallographically correct but confusing presentation of structural models deposited in the Protein Data Bank.
Dauter et al. (2018)