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PDBsum entry 2jet

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protein Protein-protein interface(s) links
Hydrolase PDB id
2jet
Jmol
Contents
Protein chains
12 a.a.
125 a.a. *
93 a.a. *
Waters ×67
* Residue conservation analysis
PDB id:
2jet
Name: Hydrolase
Title: Crystal structure of a trypsin-like mutant (s189d, a226g) chymotrypsin.
Structure: Chymotrypsinogen b chain a. Chain: a. Fragment: resides 19-28. Engineered: yes. Chymotrypsinogen b chain b. Chain: b. Fragment: residues 37-164. Engineered: yes. Chymotrypsinogen b chain c.
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Organ: pancreas. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.20Å     R-factor:   0.279     R-free:   0.334
Authors: B.Jelinek,G.Katona,K.Fodor,I.Venekei,L.Graf
Key ref: B.Jelinek et al. (2008). The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin. Protein J, 27, 79-87. PubMed id: 17805946
Date:
22-Jan-07     Release date:   18-Sep-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P07338  (CTRB1_RAT) -  Chymotrypsinogen B
Seq:
Struc:
263 a.a.
12 a.a.*
Protein chain
Pfam   ArchSchema ?
P07338  (CTRB1_RAT) -  Chymotrypsinogen B
Seq:
Struc:
263 a.a.
125 a.a.
Protein chain
Pfam   ArchSchema ?
P07338  (CTRB1_RAT) -  Chymotrypsinogen B
Seq:
Struc:
263 a.a.
93 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C: E.C.3.4.21.1  - Chymotrypsin.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     catalytic activity     2 terms  

 

 
Protein J 27:79-87 (2008)
PubMed id: 17805946  
 
 
The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin.
B.Jelinek, G.Katona, K.Fodor, I.Venekei, L.Gráf.
 
  ABSTRACT  
 
The crystal structure of the S189D+A226G rat chymotrypsin-B mutant has been determined at 2.2 angstroms resolution. This mutant is the most trypsin-like mutant so far in the line of chymotrypsin-to-trypsin conversions, aiming for a more complete understanding of the structural basis of substrate specificity in pancreatic serine proteases. A226G caused significant rearrangements relative to S189D chymotrypsin, allowing an internal conformation of Asp189 which is close to that in trypsin. Serious distortions remain, however, in the activation domain, including zymogen-like features. The pH-profile of activity suggests that the conformation of the S1-site of the mutant is influenced also by the P1 residue of the substrate.