1u10

X-ray diffraction
2.4Å resolution

MEPA, active form with ZN in P1

Released:
Source organism: Escherichia coli
Primary publication:
Peptidoglycan amidase MepA is a LAS metallopeptidase.
J. Biol. Chem. 279 43982-9 (2004)
PMID: 15292190

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Penicillin-insensitive murein endopeptidase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 255 amino acids
Theoretical weight: 28.61 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0C0T5 (Residues: 20-274; Coverage: 100%)
Gene names: JW2325, b2328, mepA
Sequence domains: Penicillin-insensitive murein endopeptidase
Structure domains: Muramoyl-pentapeptide Carboxypeptidase; domain 2

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P1
Unit cell:
a: 35.613Å b: 77.988Å c: 127.663Å
α: 93.15° β: 95.93° γ: 90.75°
R-values:
R R work R free
0.236 0.234 0.266
Expression system: Escherichia coli BL21(DE3)