1nb5

X-ray diffraction
2.4Å resolution

Crystal structure of stefin A in complex with cathepsin H

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|- bonds) as well as an endopeptidase.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-129217 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Cathepsin H Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 24.33 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: O46427 (Residues: 116-335; Coverage: 70%)
Gene name: CTSH
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
Cathepsin H mini chain Chains: P, R, S, T
Molecule details ›
Chains: P, R, S, T
Length: 8 amino acids
Theoretical weight: 849 Da
Source organism: Sus scrofa
UniProt:
  • Canonical: O46427 (Residues: 98-105; Coverage: 3%)
Gene name: CTSH
Cystatin-A Chains: I, J, K, L
Molecule details ›
Chains: I, J, K, L
Length: 98 amino acids
Theoretical weight: 11.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01040 (Residues: 1-98; Coverage: 100%)
Gene names: CSTA, STF1, STFA
Sequence domains: Cystatin domain
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 91.629Å b: 97.575Å c: 162.188Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.274
Expression system: Escherichia coli