› 1tmg

X-ray diffraction
1.67Å resolution

crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59F mutant

Released:
DOI: 10.2210/pdb1tmg/pdb
PDB entry 1tmg coloured by chain, front view.
PDB entry 1tmg coloured by chain, side view.
PDB entry 1tmg 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: 7.3 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P6522
Unit cell:
a: 94.164Å b: 94.164Å c: 185.318Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.149 0.174
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

1 mention without citation

From thiol-subtilisin to omniligase: Design and structure of a broadly applicable peptide ligase.
Toplak et al. (2021)