PDBe 1m21

X-ray diffraction
1.8Å resolution

Crystal structure analysis of the peptide amidase PAM in complex with the competitive inhibitor chymostatin

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CHYMOSTATIN Chains: C, D
Molecule details ›
Chains: C, D
Length: 4 amino acids
Theoretical weight: 608 Da
Source organism: Streptomyces hygroscopicus
Expression system: Not provided
Peptide 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 name: pam
Sequence domains: Amidase
Structure domains: Amidase signature (AS) enzymes

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 74.598Å b: 62.559Å c: 102.382Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.217
Expression systems:
  • Not provided
  • Escherichia coli