Structure of PDB 2o8j Chain B

Receptor sequence

>2o8jB (length=271) Species: 9606 (Homo sapiens)

ICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHL
QHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQAC
SCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGEL
ISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIP
VRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCG
SEKCKHSAEAIALEQSRLARL

3D structure

• PDB: 2o8j Structural biology of human H3K9 methyltransferases
• Chain: B
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y1067 Y1154
• Catalytic site (residue number reindexed from 1): Y146 Y233
• Enzyme Commision number: 2.1.1.-
  2.1.1.367: [histone H3]-lysine(9) N-methyltransferase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	B	C974 C987 C1017 C1021	C53 C66 C96 C100
BS02	ZN	B	C980 C1017 C1023 C1027	C59 C96 C102 C106
BS03	ZN	B	C974 C976 C980 C985	C53 C55 C59 C64
BS04	ZN	B	C1115 C1168 C1170 C1175	C194 C247 C249 C254
BS05	SAH	B	M1048 W1050 S1084 Y1085 R1109 F1110 N1112 H1113 Y1154 F1166 C1168 Q1169	M127 W129 S163 Y164 R188 F189 N191 H192 Y233 F245 C247 Q248

Gene Ontology

Molecular Function

• GO:0002039 p53 binding
• GO:0008270 zinc ion binding
• GO:0016279 protein-lysine N-methyltransferase activity
• GO:0042054 histone methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:2o8j, PDBe:2o8j, PDBj:2o8j
• PDBsum: 2o8j
• PubMed: 20084102
• UniProt: Q96KQ7|EHMT2_HUMAN Histone-lysine N-methyltransferase EHMT2 (Gene Name=EHMT2)