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Ligands
Code Name Style Show Link
90P N~2~-cyclohexyl-N~4~-(1-ethylpiperidin-4-yl)-6,7-dimethoxy-N~2~-methylquinazoline-2,4-diamine
CL Chloride ion
DMS Dimethyl sulfoxide
SAM S-adenosylmethionine
UNX Unknown atom or ion
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Modification
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Code : 5V9J   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal structure of catalytic domain of GLP with MS0105
Release Data : 2018-03-21
Compound :
mol_id molecule chains synonym
1 Histone-lysine N-methyltransferase EHMT1 A,B Euchromatic histone-lysine N-methyltransferase 1,Eu-HMTase1,G9a-like protein 1,GLP1,Histone H3-K9 methyltransferase 5,H3-K9-HMTase 5,Lysine N-methyltransferase 1D
ec: 2.1.1.-,2.1.1.43
fragment: residues 982-1266
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21  (taxid:511693)
gene: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D
expression_system_strain: BL21-V2R-PRARE2
expression_system_vector_type: plasmid
expression_system_plasmid: PET28-LIC
Authors : Dong, A., Zeng, H., Liu, J., Xiong, Y., Babault, N., Jin, J., Tempel, W., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Wu, H., Brown, P.J., Structural Genomics Consortium (SGC)
Keywords : EHMT1, methyltransferase, Structural Genomics, Structural Genomics Consortium, SGC, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.7400 Å )
Citation :

Crystal structure of catalytic domain of GLP with MS0105

Zeng, H.,Dong, A.,Liu, J.  et al.
to be published 

Chain : A, B
UniProt : Q9H9B1 (EHMT1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L- homocysteine - PubMed:12004135
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L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine 2.1.1.367 PubMed:12004135
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