5e2h

X-ray diffraction
1.8Å resolution

Crystal Structure of D-alanine Carboxypeptidase AmpC from Mycobacterium smegmatis

Released:
Model geometry
Fit model/data
Entry authors: Kim Y, Hatzos-Skintges C, Endres M, Babnigg G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106389 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 357 amino acids
Theoretical weight: 38.8 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli
UniProt:
  • Canonical: A0QZC8 (Residues: 27-380; Coverage: 100%)
Gene name: MSMEG_3978
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 127.779Å b: 73.682Å c: 113.413Å
α: 90° β: 90.19° γ: 90°
R-values:
R R work R free
0.165 0.164 0.197
Expression system: Escherichia coli