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PDBsum entry 5emx

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protein links
Transcription PDB id
5emx

 

 

 

 

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Contents
Protein chains
53 a.a.
54 a.a.
Waters ×78
PDB id:
5emx
Name: Transcription
Title: Crystal structure of the s. Cerevisiae rtf1 histone modification domain mutant r124a r126a r128a
Structure: RNA polymerase-associated protein rtf1. Chain: a, b. Fragment: unp residues 74-139. Engineered: yes. Mutation: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: rtf1, csl3, ygl244w, hra458. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.40Å     R-factor:   0.144     R-free:   0.178
Authors: A.D.Wier,A.Heroux,A.P.Vandemark
Key ref: S.B.Van Oss et al. (2016). The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6. Mol Cell, 64, 815-825. PubMed id: 27840029 DOI: 10.1016/j.molcel.2016.10.008
Date:
06-Nov-15     Release date:   26-Oct-16    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P53064  (RTF1_YEAST) -  RNA polymerase-associated protein RTF1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
558 a.a.
53 a.a.*
Protein chain
Pfam   ArchSchema ?
P53064  (RTF1_YEAST) -  RNA polymerase-associated protein RTF1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
558 a.a.
54 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.molcel.2016.10.008 Mol Cell 64:815-825 (2016)
PubMed id: 27840029  
 
 
The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.
S.B.Van Oss, M.K.Shirra, A.R.Bataille, A.D.Wier, K.Yen, V.Vinayachandran, I.L.Byeon, C.E.Cucinotta, A.Héroux, J.Jeon, J.Kim, A.P.VanDemark, B.F.Pugh, K.M.Arndt.
 
  ABSTRACT  
 
No abstract given.

 

 

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