4hv4

X-ray diffraction
2.25Å resolution

2.25 Angstrom resolution crystal structure of UDP-N-acetylmuramate--L-alanine ligase (murC) from Yersinia pestis CO92 in complex with AMP

Released:
Source organism: Yersinia pestis CO92
Entry authors: Halavaty AS, Minasov G, Dubrovska I, Winsor J, Shuvalova L, Peterson S, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-187210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramate--L-alanine ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 494 amino acids
Theoretical weight: 53.99 KDa
Source organism: Yersinia pestis CO92
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8ZIE8 (Residues: 1-491; Coverage: 100%)
Gene names: YPO0556, YP_3628, murC, y3625
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 66.534Å b: 78.021Å c: 183.296Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.224
Expression system: Escherichia coli BL21