Structure of PDB 4nvq Chain B

Receptor sequence

>4nvqB (length=263) Species: 9606 (Homo sapiens)

TEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRN
ITHLQHCTCVDDCSSSNCLCRCWYDKDGRLLQEFNKIEPPLIFECNQACS
CWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELI
SDAEADVREDDSYLFDLDVYCIDARYYGNISRFINHLCDPNIIPVRVFML
HQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKH
SAEAIALEQSRLA

3D structure

• PDB: 4nvq Discovery and development of potent and selective inhibitors of histone methyltransferase g9a.
• Chain: B
• Resolution: 2.03 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y1067 Y1154
• Catalytic site (residue number reindexed from 1): Y145 Y227
• 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	SAH	B	M1048 W1050 Y1085 R1109 F1110 N1112 H1113 Y1154 F1158 F1166 C1168 Q1169	M126 W128 Y163 R182 F183 N185 H186 Y227 F231 F239 C241 Q242
BS02	2OD	B	Y1067 D1074 A1077 D1078 D1083 S1084 L1086 F1087 D1088 F1152 Y1154 R1157 F1158 I1161	Y145 D152 A155 D156 D161 S162 L164 F165 D166 F225 Y227 R230 F231 I234	MOAD: ic50=3.3nM BindingDB: IC50=3.3nM
BS03	ZN	B	C980 C1017 C1023 C1027	C63 C95 C101 C105
BS04	ZN	B	C974 C976 C980 C985	C57 C59 C63 C68
BS05	ZN	B	C974 C987 C1017 C1021	C57 C70 C95 C99
BS06	ZN	B	C1115 C1168 C1170 C1175	C188 C241 C243 C248

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:4nvq, PDBe:4nvq, PDBj:4nvq
• PDBsum: 4nvq
• PubMed: 24900801
• UniProt: Q96KQ7|EHMT2_HUMAN Histone-lysine N-methyltransferase EHMT2 (Gene Name=EHMT2)