› 3m2p

X-ray diffraction
2.95Å resolution

The crystal structure of UDP-N-acetylglucosamine 4-epimerase from Bacillus cereus

Released:
DOI: 10.2210/pdb3m2p/pdb
PDB entry 3m2p coloured by chain, front view.
PDB entry 3m2p coloured by chain, side view.
PDB entry 3m2p coloured by chain, top view.
Source organism: Bacillus cereus ATCC 14579
Entry authors: Zhang Z, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed: 
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182433 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent epimerase/dehydratase domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 311 amino acids
Theoretical weight: 35.29 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q814Z6 (Residues: 2-301; Coverage: 100%)
Gene name: BC_5271
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand UDP 1 x UDP
1 modified residue:
Ligand MSE 30 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 104.116Å b: 149.725Å c: 166.326Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.212 0.276
Expression system: Escherichia coli BL21(DE3)

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