Structure of PDB 2igq Chain B

Receptor sequence

>2igqB (length=254) Species: 9606 (Homo sapiens)

ERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNI
THLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECN
HACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYV
GELISDSEADVREEDSYLFDLDEVYCIDARFYGNVSRFINHHCEPNLVPV
RVFMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKLFSCRCGSPK
CRHS

3D structure

• PDB: 2igq Structural biology of human H3K9 methyltransferases
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y1124 Y1211
• Catalytic site (residue number reindexed from 1): Y149 Y232
• 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	C1031 C1044 C1074 C1078	C56 C69 C99 C103
BS02	ZN	B	C1037 C1074 C1080 C1084	C62 C99 C105 C109
BS03	ZN	B	C1031 C1033 C1037 C1042	C56 C58 C62 C67
BS04	ZN	B	C1172 C1225 C1227 C1232	C193 C244 C246 C251
BS05	SAH	B	M1105 G1106 W1107 S1141 Y1142 R1166 F1167 N1169 H1170 Y1211 C1225 R1226	M130 G131 W132 S166 Y167 R187 F188 N190 H191 Y232 C244 R245	BindingDB: IC50=230nM

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
• GO:0046974 histone H3K9 methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:2igq, PDBe:2igq, PDBj:2igq
• PDBsum: 2igq
• PubMed: 20084102
• UniProt: Q9H9B1|EHMT1_HUMAN Histone-lysine N-methyltransferase EHMT1 (Gene Name=EHMT1)