› 1lml

X-ray diffraction
1.86Å resolution

LEISHMANOLYSIN

Released:
DOI: 10.2210/pdb1lml/pdb
PDB entry 1lml coloured by chain, front view.
PDB entry 1lml coloured by chain, side view.
PDB entry 1lml coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63).
Schlagenhauf E, Etges R, Metcalf P
Structure 6 1035-46 (1998)
PMID: 9739094

Function and Biology Details

Reaction catalysed: 
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-|-Leu-Lys-Lys-.
Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139931 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leishmanolysin Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 51.61 KDa
Source organism: Leishmania major
UniProt:
  • Canonical: P08148 (Residues: 100-577; Coverage: 85%)
Gene name: gp63
Sequence domains: Leishmanolysin
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: C2
Unit cell:
a: 106.325Å b: 90.144Å c: 70.145Å
α: 90° β: 110.54° γ: 90°
R-values:
R R work R free
0.191 0.191 0.208

Quick links

Citations

9 review citations

Structural aspects of the metzincin clan of metalloendopeptidases.
Gomis-Rüth FX. (2003)
8 more

26 mentions without citation

Meprins, membrane-bound and secreted astacin metalloproteinases.
Sterchi et al. (2008)
25 more