› 3i99

X-ray diffraction
2.2Å resolution

The crystal structure of the UDP-N-acetylenolpyruvoylglucosamine reductase from the Vibrio cholerae O1 biovar Tor

Released:
DOI: 10.2210/pdb3i99/pdb
PDB entry 3i99 coloured by chain, front view.
PDB entry 3i99 coloured by chain, side view.
PDB entry 3i99 coloured by chain, top view.
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Entry authors: Zhang R, Gu M, Peterson S, Anderson W, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed: 
UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192134 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylenolpyruvoylglucosamine reductase Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 39.81 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KV40 (Residues: 1-347; Coverage: 100%)
Gene names: VC_0318, murB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand PO4 2 x PO4
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43
Unit cell:
a: 84.334Å b: 84.334Å c: 53.335Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.168 0.223
Expression system: Escherichia coli

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