PDBe 1e8c

X-ray diffraction
2Å resolution

STRUCTURE OF MURE THE UDP-N-ACETYLMURAMYL TRIPEPTIDE SYNTHETASE FROM E. COLI

Released:

Function and Biology Details

Reaction catalysed:
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6- diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 498 amino acids
Theoretical weight: 54.4 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P22188 (Residues: 2-495; Coverage: 100%)
Gene names: JW0083, b0085, murE
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2221
Unit cell:
a: 93.465Å b: 99.69Å c: 236.146Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.23
Expression system: Escherichia coli