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Structure paper

TitleSpecificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 14, Page 689-695, Year 2007
Publish dateJun 10, 2007 (structure data deposition date)
AuthorsCouture, J.F. / Collazo, E. / Ortiz-Tello, P.A. / Brunzelle, J.S. / Trievel, R.C.
External linksNat. Struct. Mol. Biol. / PubMed:17589523
MethodsX-ray diffraction
Resolution2.047 - 2.29 Å
Structure data

PDB-2q8c:
Crystal structure of JMJD2A in ternary complex with an histone H3K9me3 peptide and 2-oxoglutarate
Method: X-RAY DIFFRACTION / Resolution: 2.047 Å

PDB-2q8d:
Crystal structure of JMJ2D2A in ternary complex with histone H3-K36me2 and succinate
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-2q8e:
Specificity and Mechanism of JMJD2A, a Trimethyllysine-Specific Histone Demethylase
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-ZN:
Unknown entry

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-HOH:
WATER

ChemComp-SIN:
SUCCINIC ACID

ChemComp-OGA:
N-OXALYLGLYCINE

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / histone demethylase / hydroxylase / jumonji / succinate / n-oxalylglycine

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