4qf5

X-ray diffraction
2.8Å resolution

Crystal structure I of MurF from Acinetobacter baumannii

Released:

Function and Biology Details

Reaction catalysed:
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl-D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 472 amino acids
Theoretical weight: 51.75 KDa
Source organism: Acinetobacter baumannii AB307-0294
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0J9X1Z8 (Residues: 1-466; Coverage: 100%)
Gene names: ABBFA_000315, ABBFA_00314, murF
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P21
Unit cell:
a: 44.559Å b: 89.716Å c: 126.896Å
α: 90° β: 93.45° γ: 90°
R-values:
R R work R free
0.195 0.192 0.249
Expression system: Escherichia coli