› 1bpm

X-ray diffraction
2.9Å resolution

DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY

Released:
DOI: 10.2210/pdb1bpm/pdb
PDB entry 1bpm coloured by chain, front view.
PDB entry 1bpm coloured by chain, side view.
PDB entry 1bpm coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography.
Kim H, Lipscomb WN
Proc Natl Acad Sci U S A 90 5006-10 (1993)
PMID: 8506345

Function and Biology Details

Reactions catalysed: 
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of N-terminal proline from a peptide.
An (L-cysteinylglycine)-S-conjugate + H(2)O = an L-cysteine-S-conjugate + glycine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosol aminopeptidase Chain: A
Molecule details ›
Chain: A
Length: 487 amino acids
Theoretical weight: 52.94 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00727 (Residues: 33-519; Coverage: 94%)
Gene name: LAP3
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6322
Unit cell:
a: 129.1Å b: 129.1Å c: 120.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Glutathione Degradation.
Bachhawat et al. (2017)
2 more

2 mentions without citation

Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families.
Pascual Alonso et al. (2023)
1 more