Structure of PDB 2r3a Chain A

Receptor sequence

>2r3aA (length=270) Species: 9606 (Homo sapiens)

AEYIVKKAKQRIALQRWQDELNRRKNHKGMIFVENTVDLEGPPSDFYYIN
EYKPAPGISLVTFGCSCTDCFFQKCCPAEAGVLLAYNKNQQIKIPPGTPI
YECNSRCQCGPDCPNRIVQKGTQYSLCIFRTSNGRGWGVKTLVKIKRMSF
VMEYVGEVITSEEAERRGQFYDNKGITYLFDLDYESDEFTVDAARYGNVS
HFVNHSCDPNLQVFNVFIDNLDTRLPRIALFSTRTINAGEELTFDYQMKG
SGRVRTVCKCGAVTCRGYLN

3D structure

• PDB: 2r3a Structural biology of human H3K9 methyltransferases
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y169 Y261
• Catalytic site (residue number reindexed from 1): Y154 Y246
• Enzyme Commision number: 2.1.1.355: [histone H3]-lysine(9) N-trimethyltransferase.

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	A	C222 C287 C289 C294	C207 C258 C260 C265
BS02	ZN	A	C80 C82 C85 C90	C65 C67 C70 C75
BS03	ZN	A	C80 C118 C122	C65 C103 C107
BS04	ZN	A	C85 C118 C124 C128	C70 C103 C109 C113
BS05	SAM	A	R150 G151 W152 K189 T192 Y193 H216 F217 N219 H220 Y261 C287 K288 L298	R135 G136 W137 K174 T177 Y178 H201 F202 N204 H205 Y246 C258 K259 L269
BS06	SER	A	D84 C85	D69 C70

Gene Ontology

Molecular Function

• GO:0008270 zinc ion binding
• GO:0042054 histone methyltransferase activity
• GO:0046974 histone H3K9 methyltransferase activity

Cellular Component

• GO:0005634 nucleus

External links

• PDB: RCSB:2r3a, PDBe:2r3a, PDBj:2r3a
• PDBsum: 2r3a
• PubMed: 20084102
• UniProt: Q9H5I1|SUV92_HUMAN Histone-lysine N-methyltransferase SUV39H2 (Gene Name=SUV39H2)