PDBe 1stf

X-ray diffraction
2.37Å resolution

THE REFINED 2.4 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF RECOMBINANT HUMAN STEFIN B IN COMPLEX WITH THE CYSTEINE PROTEINASE PAPAIN: A NOVEL TYPE OF PROTEINASE INHIBITOR INTERACTION

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Papain Chain: E
Molecule details ›
Chain: E
Length: 212 amino acids
Theoretical weight: 23.51 KDa
Source organism: Carica papaya
Expression system: Escherichia coli
UniProt:
  • Canonical: P00784 (Residues: 134-345; Coverage: 65%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Cystatin-B Chain: I
Molecule details ›
Chain: I
Length: 98 amino acids
Theoretical weight: 11.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04080 (Residues: 1-98; Coverage: 100%)
Gene names: CST6, CSTB, STFB
Sequence domains: Cystatin domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 67Å b: 67Å c: 169.3Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Escherichia coli