› 1m21

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb1m21/pdb
PDB entry 1m21 coloured by chain, front view.
PDB entry 1m21 coloured by chain, side view.
PDB entry 1m21 coloured by chain, top view.
Source organisms:
Primary publication:
An alternative mechanism for amidase signature enzymes.
Labahn J, Neumann S, Büldt G, Kula MR, Granzin J
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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162305 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: 93%)
Gene name: pam
Sequence domains: Amidase
Structure domains: Amidase signature (AS) domain
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

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PHA 2 x PHA

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:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

Structure and function of fatty acid amide hydrolase.
McKinney et al. (2005)
5 more

5 mentions without citation

Binding and inactivation mechanism of a humanized fatty acid amide hydrolase by alpha-ketoheterocycle inhibitors revealed from cocrystal structures.
Mileni et al. (2009)
4 more