PDBe 1m22

X-ray diffraction
1.4Å resolution

X-ray structure of native peptide amidase from Stenotrophomonas maltophilia at 1.4 A

Released:
Source organism: Stenotrophomonas maltophilia
Primary publication:
An alternative mechanism for amidase signature enzymes.
J. Mol. Biol. 322 1053-64 (2002)
PMID: 12367528

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 503 amino acids
Theoretical weight: 53.55 KDa
Source organism: Stenotrophomonas maltophilia
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8RJN5 (Residues: 38-540; Coverage: 99%)
Gene names: DM611_04005, pam
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 74.179Å b: 62.596Å c: 101.906Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.188 0.199
Expression system: Escherichia coli