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PDBsum entry 4dm6

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protein ligands Protein-protein interface(s) links
Transcription/protein binding PDB id
4dm6

 

 

 

 

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Contents
Protein chains
240 a.a.
11 a.a.
12 a.a.
Ligands
TTB ×2
Waters ×178
PDB id:
4dm6
Name: Transcription/protein binding
Title: Crystal structure of rarb lbd homodimer in complex with ttnpb
Structure: Retinoic acid receptor beta. Chain: a, b. Fragment: unp residues 176-421. Synonym: rar-beta, hbv-activated protein, nuclear receptor subfamily 1 group b member 2, rar-epsilon. Engineered: yes. Nuclear receptor coactivator 1. Chain: e, f. Fragment: unp residues 676-700.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: rarb, hap, nr1b2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
Resolution:
1.90Å     R-factor:   0.206     R-free:   0.239
Authors: J.Osz,Y.Brelivet,C.Peluso-Iltis,V.Cura,S.Eiler,M.Ruff,W.Bourguet, N.Rochel,D.Moras
Key ref: J.Osz et al. (2012). Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors. Proc Natl Acad Sci U S A, 109, E588. PubMed id: 22355136
Date:
07-Feb-12     Release date:   07-Mar-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10826  (RARB_HUMAN) -  Retinoic acid receptor beta from Homo sapiens
Seq:
Struc:
455 a.a.
240 a.a.
Protein chain
Pfam   ArchSchema ?
Q15788  (NCOA1_HUMAN) -  Nuclear receptor coactivator 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1441 a.a.
11 a.a.
Protein chain
Pfam   ArchSchema ?
Q15788  (NCOA1_HUMAN) -  Nuclear receptor coactivator 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1441 a.a.
12 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains E, F: 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(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Proc Natl Acad Sci U S A 109:E588 (2012)
PubMed id: 22355136  
 
 
Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors.
J.Osz, Y.Brélivet, C.Peluso-Iltis, V.Cura, S.Eiler, M.Ruff, W.Bourguet, N.Rochel, D.Moras.
 
  ABSTRACT  
 
No abstract given.

 

 

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