PDBe 1s2k

X-ray diffraction
2Å resolution

Structure of SCP-B a member of the Eqolisin family of Peptidases in a complex with a Tripeptide Ala-Ile-His

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity, cleaving 24-Phe-|-Phe-25, but not 15-Leu-|-Tyr-16 and 25-Phe-|-Tyr-26 in the B chain of insulin. 
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Scytalidopepsin B Chain: A
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 21.55 KDa
Source organism: Scytalidium lignicola
Expression system: Escherichia coli
UniProt:
  • Canonical: P15369 (Residues: 55-260; Coverage: 86%)
Sequence domains: Peptidase A4 family
Ala-Ile-His tripeptide Chain: B
Molecule details ›
Chain: B
Length: 3 amino acids
Theoretical weight: 340 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200HB
Spacegroup: P6322
Unit cell:
a: 109.369Å b: 109.369Å c: 113.829Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.234 0.256
Expression systems:
  • Escherichia coli
  • Not provided