1bll

X-ray diffraction
2.4Å resolution

X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE

Released:

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.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dodecamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cytosol aminopeptidase Chain: E
Molecule details ›
Chain: E
Length: 488 amino acids
Theoretical weight: 52.97 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00727 (Residues: 33-519; Coverage: 94%)
Gene name: LAP3
Sequence domains: Cytosol aminopeptidase family, catalytic domain
Structure domains:
AMASTATIN Chain: I
Molecule details ›
Chain: I
Length: 4 amino acids
Theoretical weight: 475 Da
Source organism: Streptomyces sp. ME98-M3
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6322
Unit cell:
a: 130.3Å b: 130.3Å c: 121.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 not available
Expression system: Not provided