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4MI0

Human Enhancer of Zeste (Drosophila) Homolog 2(EZH2)

Summary for 4MI0
Entry DOI10.2210/pdb4mi0/pdb
DescriptorHistone-lysine N-methyltransferase EZH2, ZINC ION, UNKNOWN ATOM OR ION, ... (4 entities in total)
Functional Keywordsezh2, gene regulation, chromatin modification, histone methyltransferase, transcription, gene silencing, polycomb repressive complex 2, structural genomics, structural genomics consortium, sgc, transferase
Biological sourceHomo sapiens (human)
Cellular locationNucleus : Q15910
Total number of polymer chains1
Total formula weight27098.87
Authors
Dong, A.,Zeng, H.,He, H.,Wernimont, A.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Brown, P.J.,Wu, H.,Structural Genomics Consortium (SGC) (deposition date: 2013-08-30, release date: 2013-09-25, Last modification date: 2024-02-28)
Primary citationWu, H.,Zeng, H.,Dong, A.,Li, F.,He, H.,Senisterra, G.,Seitova, A.,Duan, S.,Brown, P.J.,Vedadi, M.,Arrowsmith, C.H.,Schapira, M.
Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations.
Plos One, 8:e83737-e83737, 2013
Cited by
PubMed: 24367611
DOI: 10.1371/journal.pone.0083737
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

218500

數據於2024-04-17公開中

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