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PDBsum entry 2y0b

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protein ligands Protein-protein interface(s) links
Hydrolase/protein binding PDB id
2y0b

 

 

 

 

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Contents
Protein chains
141 a.a.
94 a.a.
119 a.a.
Ligands
MPD ×2
MRD ×2
Waters ×345
PDB id:
2y0b
Name: Hydrolase/protein binding
Title: Caspase-3 in complex with an inhibitory darpin-3.4_s76r
Structure: Caspase-3 subunit p17. Chain: a, c. Synonym: caspase-3, casp-3, apopain, cysteine protease cpp32, cpp-32, protein yama, srebp cleavage activity 1, sca-1. Engineered: yes. Caspase-3. Chain: b, d. Synonym: caspase-3, casp-3, apopain, cysteine protease cpp32, cpp-32, protein yama, srebp cleavage activity 1, sca-1.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: t7 promoter expression. Synthetic construct. Organism_taxid: 32630. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.193     R-free:   0.217
Authors: J.Barandun,T.Schroeder,P.Mittl,M.G.Grutter
Key ref: T.Schroeder et al. (2013). Specific inhibition of caspase-3 by a competitive DARPin: molecular mimicry between native and designed inhibitors. Structure, 21, 277-289. PubMed id: 23333429
Date:
01-Dec-10     Release date:   21-Dec-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P42574  (CASP3_HUMAN) -  Caspase-3 from Homo sapiens
Seq:
Struc:
277 a.a.
141 a.a.*
Protein chains
Pfam   ArchSchema ?
P42574  (CASP3_HUMAN) -  Caspase-3 from Homo sapiens
Seq:
Struc:
277 a.a.
94 a.a.
Protein chains
No UniProt id for this chain
Struc: 119 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.3.4.22.56  - caspase-3.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Structure 21:277-289 (2013)
PubMed id: 23333429  
 
 
Specific inhibition of caspase-3 by a competitive DARPin: molecular mimicry between native and designed inhibitors.
T.Schroeder, J.Barandun, A.Flütsch, C.Briand, P.R.Mittl, M.G.Grütter.
 
  ABSTRACT  
 
No abstract given.

 

 

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