Het-PDB Navi2 (PDB: 1O9S)

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Ligands
Code	Name		Style	Show	Link
SAH	S-adenosyl-L-homocysteine				PoSSuM

Non-standard Residues
Code	Name	Show
MLZ	N-methyl-lysine

Glycosylation
Code	Name	Emphasize

Modification
Code	Name	Show

Download interaction data: 1O9S

Code :

1O9S PDBj RCSB PDB PDBe

Header :

TRANSFERASE

Title :

Crystal structure of a ternary complex of the human histone methyltransferase SET7/9

Release Data :

2003-02-06

Compound :

mol_id	molecule	chains	synonym
1	HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-4 SPECIFIC	A,B	HISTONE H3-K4 METHYLTRANSFERASE, H3-K4-HMTASE
	ec: 2.1.1.43 fragment: N-DOMAIN, SET-DOMAIN, RESIDUES 108-366

mol_id	molecule	chains
2	GENE FRAGMENT FOR HISTONE H3	K,L
	fragment: RESIDUES 2-11

Source :

mol_id	organism_scientific	organism_common	expression_system
1	HOMO SAPIENS (taxid:9606)	HUMAN	ESCHERICHIA COLI (taxid:562)

mol_id	organism_scientific	organism_common
2	HOMO SAPIENS (taxid:9606)	HUMAN
	synthetic: yes

Authors :

Xiao, B., Jing, C., Wilson, J.R., Walker, P.A., Vasisht, N., Kelly, G., Howell, S., Taylor, I.A., Blackburn, G.M., Gamblin, S.J.

Keywords :

METHYLATION, HISTONE H3, METHYLTRANSFERASE, TRANSFERASE

Exp. method :

X-RAY DIFFRACTION ( 1.75 Å )

Citation :

Structure and Catalytic Mechanism of the Human Histone Methyltransferase Set7/9

Xiao, B.,Jing, C.,Wilson, J.R. et al.
(2003) Nature 421 : 652

Chain :

A, B

UniProt :

Q8WTS6 (SETD7_HUMAN)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine	2.1.1.364	PROSITE-ProRule:PRU00910, PubMed:12540855
	-	PROSITE-ProRule:PRU00910, PubMed:12540855
L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)- methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine	-	PubMed:15099517, PubMed:15525938, PubMed:16415881
	left-to-right	PubMed:15099517, PubMed:15525938, PubMed:16415881

PDB ID: 1O9S