PDBe 1lml

X-ray diffraction
1.86Å resolution

LEISHMANOLYSIN

Released:

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)
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
Structure domains:

Ligands and Environments

1 bound ligand:

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