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PDBsum entry 3opt

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protein ligands metals links
Oxidoreductase PDB id
3opt

 

 

 

 

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Contents
Protein chain
298 a.a. *
Ligands
AKG
Metals
_NI
Waters ×226
* Residue conservation analysis
PDB id:
3opt
Name: Oxidoreductase
Title: Crystal structure of the rph1 catalytic core with a-ketoglutarate
Structure: DNA damage-responsive transcriptional repressor rph1. Chain: a. Fragment: catalytic core domain, unp residues 1-373. Engineered: yes
Source: Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: rph1, yer169w. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.20Å     R-factor:   0.200     R-free:   0.236
Authors: Y.Chang,J.Wu,X.Tong,J.Zhou,J.Ding
Key ref: Y.Chang et al. (2011). Crystal structure of the catalytic core of Saccharomyces cerevesiae histone demethylase Rph1: insights into the substrate specificity and catalytic mechanism. Biochem J, 433, 295-302. PubMed id: 21067515
Date:
02-Sep-10     Release date:   22-Dec-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P39956  (RPH1_YEAST) -  DNA damage-responsive transcriptional repressor RPH1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
796 a.a.
298 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.14.11.27  - [histone H3]-dimethyl-L-lysine(36) demethylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6,N6-dimethyl-L-lysyl36-[histone H3] + 2 2-oxoglutarate + 2 O2 = L-lysyl36-[histone H3] + 2 formaldehyde + 2 succinate + 2 CO2
N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
Bound ligand (Het Group name = AKG)
corresponds exactly
+ 2 × 2-oxoglutarate
+ 2 × O2
= L-lysyl(36)-[histone H3]
+ 2 × formaldehyde
+ 2 × succinate
+ 2 × CO2
      Cofactor: Fe(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Biochem J 433:295-302 (2011)
PubMed id: 21067515  
 
 
Crystal structure of the catalytic core of Saccharomyces cerevesiae histone demethylase Rph1: insights into the substrate specificity and catalytic mechanism.
Y.Chang, J.Wu, X.J.Tong, J.Q.Zhou, J.Ding.
 
  ABSTRACT  
 
No abstract given.

 

 

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