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PDBsum entry 4m7c

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protein Protein-protein interface(s) links
Hydrolase regulator PDB id
4m7c

 

 

 

 

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Contents
Protein chains
195 a.a.
13 a.a.
Waters ×271
PDB id:
4m7c
Name: Hydrolase regulator
Title: Crystal structure of the trf2-binding motif of slx4 in complex with the trfh domain of trf2
Structure: Telomeric repeat-binding factor 2. Chain: a, b. Fragment: trfh domain, unp residues 45-244. Synonym: ttaggg repeat-binding factor 2, telomeric DNA-binding protein. Engineered: yes. Peptide from structure-specific endonuclease subunit slx4. Chain: c, d. Fragment: trf2-binding motif, unp residues 1014-1025.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: terf2, trbf2, trf2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.05Å     R-factor:   0.217     R-free:   0.262
Authors: B.Wan,Y.Chen,J.Wu,Y.Liu,M.Lei
Key ref: B.Wan et al. (2013). SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres. Cell Rep, 4, 861-869. PubMed id: 24012755 DOI: 10.1016/j.celrep.2013.08.017
Date:
12-Aug-13     Release date:   25-Sep-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q15554  (TERF2_HUMAN) -  Telomeric repeat-binding factor 2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
542 a.a.
195 a.a.
Protein chains
Pfam   ArchSchema ?
Q8IY92  (SLX4_HUMAN) -  Structure-specific endonuclease subunit SLX4 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1834 a.a.
13 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.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.celrep.2013.08.017 Cell Rep 4:861-869 (2013)
PubMed id: 24012755  
 
 
SLX4 assembles a telomere maintenance toolkit by bridging multiple endonucleases with telomeres.
B.Wan, J.Yin, K.Horvath, J.Sarkar, Y.Chen, J.Wu, K.Wan, J.Lu, P.Gu, E.Y.Yu, N.F.Lue, S.Chang, Y.Liu, M.Lei.
 
  ABSTRACT  
 
No abstract given.

 

 

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