3h6s

X-ray diffraction
2.22Å resolution

Structure of clitocypin - cathepsin V complex

Released:
Primary publication:
Versatile loops in mycocypins inhibit three protease families.
J Biol Chem 285 308-16 (2010)
PMID: 19846555

Function and Biology Details

Reaction catalysed:
The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-130199 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cathepsin L2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 221 amino acids
Theoretical weight: 24.09 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: O60911 (Residues: 114-334; Coverage: 70%)
Gene names: CATL2, CTSL2, CTSU, CTSV, UNQ268/PRO305
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Clitocypin-5 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 152 amino acids
Theoretical weight: 16.91 KDa
Source organism: Clitocybe nebularis
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q3Y9I6 (Residues: 1-152; Coverage: 100%)
Gene name: clt5
Sequence domains: Peptidase inhibitor clitocypin
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21212
Unit cell:
a: 97.18Å b: 177.76Å c: 96.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.182 0.239
Expression system: Komagataella pastoris