› 2pbh

X-ray diffraction
3.3Å resolution

CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN B AT 3.3 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb2pbh/pdb
PDB entry 2pbh coloured by chain, front view.
PDB entry 2pbh coloured by chain, side view.
PDB entry 2pbh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide.
Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V
FEBS Lett 384 211-4 (1996)
PMID: 8617355

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|- bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139795 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cathepsin B Chain: A
Molecule details ›
Chain: A
Length: 317 amino acids
Theoretical weight: 35.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07858 (Residues: 18-333; Coverage: 98%)
Gene names: CPSB, CTSB
Sequence domains:
Structure domains: Cysteine proteinases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6522
Unit cell:
a: 78.75Å b: 78.75Å c: 153.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.231 0.269
Expression system: Escherichia coli

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Citations

17 review citations

Cysteine cathepsins: from structure, function and regulation to new frontiers.
Turk et al. (2012)
16 more

2 mentions without citation

A base measure of precision for protein stability predictors: structural sensitivity.
Caldararu et al. (2021)
1 more