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PDBsum entry 5ibc

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
5ibc

 

 

 

 

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Contents
Protein chain
241 a.a.
Ligands
ACE-ASP-GLU-VAL-
ASP-0QE
Metals
_NA
Waters ×256
PDB id:
5ibc
Name: Hydrolase/hydrolase inhibitor
Title: Caspase 3 v266i
Structure: Caspase-3. Chain: a. Synonym: casp-3,apopain,cysteine protease cpp32,cpp-32,protein yama, srebp cleavage activity 1,sca-1. Engineered: yes. Mutation: yes. Ace-asp-glu-val-ask. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: casp3, cpp32. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Unidentified. Organism_taxid: 32644
Resolution:
1.66Å     R-factor:   0.175     R-free:   0.208
Authors: J.J.Maciag,S.H.Mackenzie,M.B.Tucker,J.L.Schipper,P.D.Swartz,A.C.Clark
Key ref: J.J.Maciag et al. (2016). Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection. Proc Natl Acad Sci U S A, 113, E6080. PubMed id: 27681633 DOI: 10.1073/pnas.1603549113
Date:
22-Feb-16     Release date:   26-Oct-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P42574  (CASP3_HUMAN) -  Caspase-3 from Homo sapiens
Seq:
Struc:
277 a.a.
241 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

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

 

 
DOI no: 10.1073/pnas.1603549113 Proc Natl Acad Sci U S A 113:E6080 (2016)
PubMed id: 27681633  
 
 
Tunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selection.
J.J.Maciag, S.H.Mackenzie, M.B.Tucker, J.L.Schipper, P.Swartz, A.C.Clark.
 
  ABSTRACT  
 
No abstract given.

 

 

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