› 1to2

X-ray diffraction
1.3Å resolution

crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59K, in pH 9 cryosoak

Released:
DOI: 10.2210/pdb1to2/pdb
PDB entry 1to2 coloured by chain, front view.
PDB entry 1to2 coloured by chain, side view.
PDB entry 1to2 coloured by chain, top view.
Source organisms:
Primary publication:
Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex.
Radisky ES, Kwan G, Karen Lu CJ, Koshland DE
Biochemistry 43 13648-56 (2004)
PMID: 15504027

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133535 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Subtilisin BPN' Chain: E
Molecule details ›
Chain: E
Length: 281 amino acids
Theoretical weight: 28.38 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P00782 (Residues: 108-382; Coverage: 78%)
Gene name: apr
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain
Chymotrypsin inhibitor 2 Chain: I
Molecule details ›
Chain: I
Length: 64 amino acids
Theoretical weight: 7.28 KDa
Source organism: Hordeum vulgare subsp. vulgare
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q40059 (Residues: 21-84; Coverage: 76%)
Gene name: Ica-2
Sequence domains: Potato inhibitor I family
Structure domains: Trypsin Inhibitor V, subunit A

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand NA 1 x NA
Ligand CIT 2 x CIT
Ligand 15P 3 x 15P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P6522
Unit cell:
a: 93.671Å b: 93.671Å c: 185.92Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.169 0.168 0.183
Expression systems:
  • Bacillus subtilis
  • Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Action of plant proteinase inhibitors on enzymes of physiopathological importance.
Oliva et al. (2009)
1 more

11 mentions without citation

Rapid genome reshaping by multiple-gene loss after whole-genome duplication in teleost fish suggested by mathematical modeling.
Inoue et al. (2015)
10 more