› 3czx

X-ray diffraction
1.6Å resolution

The crystal structure of the putative N-acetylmuramoyl-L-alanine amidase from Neisseria meningitidis

Released:
DOI: 10.2210/pdb3czx/pdb
PDB entry 3czx coloured by chain, front view.
PDB entry 3czx coloured by chain, side view.
PDB entry 3czx coloured by chain, top view.
Source organism: Neisseria meningitidis MC58
Entry authors: Zhang R, Zhou M, Bargassa M, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed: 
Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylmuramoyl-L-alanine amidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 182 amino acids
Theoretical weight: 19.59 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9JZE9 (Residues: 1-181; Coverage: 100%)
Gene name: NMB1085
Sequence domains: N-acetylmuramoyl-L-alanine amidase
Structure domains: Zn-dependent exopeptidases

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 67.955Å b: 65.039Å c: 79.319Å
α: 90° β: 109.53° γ: 90°
R-values:
R R work R free
0.182 0.18 0.218
Expression system: Escherichia coli BL21

Quick links