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PDBsum entry 4ehf

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protein ligands links
Hydrolase/hydrolase inhibitor PDB id
4ehf

 

 

 

 

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Contents
Protein chain
242 a.a.
Ligands
ACE-ASP-GLU-VAL-
ASP-0QE
Waters ×207
PDB id:
4ehf
Name: Hydrolase/hydrolase inhibitor
Title: Allosteric modulation of caspase-3 through mutagenesis
Structure: Caspase-3. Chain: a. Synonym: casp-3, apopain, cysteine protease cpp32, cpp-32, protein yama, srebp cleavage activity 1, sca-1, caspase-3 subunit p17, caspase-3 subunit p12. Engineered: yes. Mutation: yes. Ace-asp-glu-val-asp-chloromethylketone inhibitor. Chain: b.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: casp3, cpp32. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
Resolution:
1.66Å     R-factor:   0.163     R-free:   0.185
Authors: J.Walters,J.L.Schipper,P.D.Swartz,C.Mattos,A.C.Clark
Key ref: J.Walters et al. (2012). Allosteric modulation of caspase 3 through mutagenesis. Biosci Rep, 32, 401-411. PubMed id: 22607239
Date:
02-Apr-12     Release date:   06-Jun-12    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P42574  (CASP3_HUMAN) -  Caspase-3 from Homo sapiens
Seq:
Struc:
277 a.a.
242 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.56  - caspase-3.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Biosci Rep 32:401-411 (2012)
PubMed id: 22607239  
 
 
Allosteric modulation of caspase 3 through mutagenesis.
J.Walters, J.L.Schipper, P.Swartz, C.Mattos, A.C.Clark.
 
  ABSTRACT  
 
No abstract given.

 

 

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