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PDBsum entry 3uv4

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protein ligands Protein-protein interface(s) links
Transcription PDB id
3uv4

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
125 a.a.
Ligands
EDO ×3
GOL
PO4
Waters ×305
PDB id:
3uv4
Name: Transcription
Title: Crystal structure of the second bromodomain of human transcription initiation factor tfiid subunit 1 (taf1)
Structure: Second bromodomain of human transcription initiation factor tfiid subunit 1 (taf1). Chain: a, b. Fragment: unp residues 1501-1635. Synonym: cell cycle gene 1 protein, tbp-associated factor 250 kda, p250, transcription initiation factor tfiid 250 kda subunit, taf(ii) 250, tafii-250, tafii250. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ba2r, ccg1, ccgs, taf1, taf2a. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.89Å     R-factor:   0.192    
Authors: P.Filippakopoulos,S.Picaud,T.Keates,E.Ugochukwu,F.Von Delft, C.H.Arrowsmith,A.M.Edwards,J.Weigelt,C.Bountra,S.Knapp,Structural Genomics Consortium (Sgc)
Key ref: P.Filippakopoulos et al. (2012). Histone recognition and large-scale structural analysis of the human bromodomain family. Cell, 149, 214-231. PubMed id: 22464331
Date:
29-Nov-11     Release date:   14-Mar-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21675  (TAF1_HUMAN) -  Transcription initiation factor TFIID subunit 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1872 a.a.
125 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.2.3.1.48  - histone acetyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
L-lysyl-[protein]
+ acetyl-CoA
= N(6)-acetyl-L-lysyl-[protein]
+ CoA
+ H(+)
   Enzyme class 2: E.C.2.7.11.1  - non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction:
1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
L-seryl-[protein]
+ ATP
= O-phospho-L-seryl-[protein]
+ ADP
+ H(+)
L-threonyl-[protein]
+ ATP
= O-phospho-L-threonyl-[protein]
+ ADP
+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Cell 149:214-231 (2012)
PubMed id: 22464331  
 
 
Histone recognition and large-scale structural analysis of the human bromodomain family.
P.Filippakopoulos, S.Picaud, M.Mangos, T.Keates, J.P.Lambert, D.Barsyte-Lovejoy, I.Felletar, R.Volkmer, S.Müller, T.Pawson, A.C.Gingras, C.H.Arrowsmith, S.Knapp.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23211769 C.A.Musselman, M.E.Lalonde, J.Côté, and T.G.Kutateladze (2012).
Perceiving the epigenetic landscape through histone readers.
  Nat Struct Mol Biol, 19, 1218-1227.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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