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PDBsum entry 4fbk

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protein ligands metals Protein-protein interface(s) links
Hydrolase, protein binding PDB id
4fbk

 

 

 

 

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Contents
Protein chains
424 a.a.
Ligands
SO4 ×4
Metals
_MN ×2
Waters ×210
PDB id:
4fbk
Name: Hydrolase, protein binding
Title: Crystal structure of a covalently fused nbs1-mre11 complex with one manganese ion per active site
Structure: DNA repair and telomere maintenance protein nbs1,DNA repair protein rad32 chimeric protein. Chain: a, b. Fragment: unp o43070 residues 474-531, unp q09683 residues 15-413. Engineered: yes
Source: Schizosaccharomyces pombe. Organism_taxid: 4896. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.38Å     R-factor:   0.223     R-free:   0.242
Authors: C.B.Schiller,K.Lammens,K.P.Hopfner
Key ref: C.B.Schiller et al. (2012). Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat Struct Biol, 19, 693-700. PubMed id: 22705791
Date:
23-May-12     Release date:   20-Jun-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
O43070  (NBS1_SCHPO) -  DNA repair and telomere maintenance protein nbs1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Seq:
Struc:
 
Seq:
Struc:
613 a.a.
424 a.a.*
Protein chains
Pfam   ArchSchema ?
Q09683  (RAD32_SCHPO) -  Double-strand break repair protein rad32 from Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Seq:
Struc:
 
Seq:
Struc:
649 a.a.
424 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 113 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Nat Struct Biol 19:693-700 (2012)
PubMed id: 22705791  
 
 
Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling.
C.B.Schiller, K.Lammens, I.Guerini, B.Coordes, H.Feldmann, F.Schlauderer, C.Möckel, A.Schele, K.Strässer, S.P.Jackson, K.P.Hopfner.
 
  ABSTRACT  
 
No abstract given.

 

 

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