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PDBsum entry 3uvl

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protein ligands links
Transcription PDB id
3uvl

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
303 a.a.
Ligands
GLY-SER-ALA-ARG-
ALA-GLU-PRO-LYS-
MET
Waters ×180
PDB id:
3uvl
Name: Transcription
Title: Crystal structure of wdr5 in complex with the wdr5-interacting motif of mll3
Structure: Wd repeat-containing protein 5. Chain: a. Fragment: unp residues 21-334. Synonym: wdr5, bmp2-induced 3-kb gene protein. Engineered: yes. Histone-lysine n-methyltransferase mll3. Chain: b. Fragment: wdr5-interacting motif (unp residues 4707-4717). Synonym: homologous to alr protein, lysine n-methyltransferase 2c,
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: wdr5, big3. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606
Resolution:
2.20Å     R-factor:   0.172     R-free:   0.220
Authors: P.Zhang,H.Lee,J.S.Brunzelle,J.-F.Couture
Key ref: P.Zhang et al. (2012). The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases. Nucleic Acids Res, 40, 4237-4246. PubMed id: 22266653
Date:
30-Nov-11     Release date:   14-Dec-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P61964  (WDR5_HUMAN) -  WD repeat-containing protein 5 from Homo sapiens
Seq:
Struc:
334 a.a.
303 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.43  - Transferred entry: 2.1.1.354.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone]
S-adenosyl-L-methionine
+ L-lysine-[histone]
= S-adenosyl-L-homocysteine
+ N(6)-methyl-L-lysine-[histone]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Nucleic Acids Res 40:4237-4246 (2012)
PubMed id: 22266653  
 
 
The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases.
P.Zhang, H.Lee, J.S.Brunzelle, J.F.Couture.
 
  ABSTRACT  
 
No abstract given.

 

 

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