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Ligands
Code Name Style Show Link
NI Nickel (II) ion
ZN Zinc ion
OGA N-oxalylglycine
Non-standard Residues
Code Name Show
M3L N-trimethyllysine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 2Q8E   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Specificity and Mechanism of JMJD2A, a Trimethyllysine-Specific Histone Demethylase
Release Data : 2007-07-03
Compound :
mol_id molecule chains synonym
1 JmjC domain-containing histone demethylation protein 3A A,B Jumonji domain-containing protein 2A
ec: 1.14.11.-
fragment: Jumonji domain
mol_id molecule chains
2 histone 3 peptide F,G
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21  (taxid:511693)
gene: JMJD2A, JHDM3A, JMJD2, KIAA0677
expression_system_strain: Bl-21
expression_system_vector_type: plasmid
expression_system_plasmid: pET15b
mol_id organism_scientific
2
synthetic: yes
other_details: Synthetic Peptide
Authors : Couture, J.-F., Collazo, E., Ortiz-Tello, P., Brunzelle, J.S., Trievel, R.C.
Keywords : histone demethylase, hydroxylase, n-oxalylglycine, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.05 Å )
Citation :

Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase.

Couture, J.F.,Collazo, E.,Ortiz-Tello, P.A.  et al.
(2007)  Nat.Struct.Mol.Biol.  14 : 689 - 695

PubMed: 17589523
DOI: 10.1038/nsmb1273

Chain : A, B
UniProt : O75164 (KDM4A_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)- [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L- lysyl(9)-[histone H3] + 2 succinate 1.14.11.66 PubMed:16603238
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2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)- [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L- lysyl(36)-[histone H3] + 2 succinate 1.14.11.69 PubMed:16603238
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