2hc9

X-ray diffraction
1.85Å resolution

Structure of Caenorhabditis elegans leucine aminopeptidase-zinc complex (LAP1)

Released:
Source organism: Caenorhabditis elegans
Entry authors: Zhan C, Patskovsky Y, Wengerter BC, Ramagopal U, Milstein S, Vidal M, Almo SC, Burley SK, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction 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.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-152708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine aminopeptidase 1 Chain: A
Molecule details ›
Chain: A
Length: 491 amino acids
Theoretical weight: 52.48 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P34629 (Residues: 1-491; Coverage: 100%)
Gene names: ZK353.6, lap-1
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6322
Unit cell:
a: 131.309Å b: 131.309Å c: 126.344Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.142 0.175
Expression system: Escherichia coli