› 2jet

X-ray diffraction
2.2Å resolution

Crystal structure of a trypsin-like mutant (S189D , A226G) chymotrypsin.

Released:
DOI: 10.2210/pdb2jet/pdb
PDB entry 2jet coloured by chain, front view.
PDB entry 2jet coloured by chain, side view.
PDB entry 2jet coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin.
Jelinek B, Katona G, Fodor K, Venekei I, Gráf L
Protein J 27 79-87 (2008)
PMID: 17805946

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139520 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Chymotrypsin B chain A Chain: A
Molecule details ›
Chain: A
Length: 15 amino acids
Theoretical weight: 1.54 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07338 (Residues: 15-28; Coverage: 4%)
Gene names: Ctrb, Ctrb1
Chymotrypsin B chain B Chain: B
Molecule details ›
Chain: B
Length: 128 amino acids
Theoretical weight: 13.88 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07338 (Residues: 37-164; Coverage: 52%)
Gene names: Ctrb, Ctrb1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Chymotrypsin B chain C Chain: C
Molecule details ›
Chain: C
Length: 99 amino acids
Theoretical weight: 10.25 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07338 (Residues: 165-263; Coverage: 40%)
Gene names: Ctrb, Ctrb1
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 34.69Å b: 64.351Å c: 44.224Å
α: 90° β: 102.09° γ: 90°
R-values:
R R work R free
0.279 0.276 0.334
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Conformational selection in trypsin-like proteases.
Pozzi et al. (2012)
1 other article