Structure of PDB 2igq Chain A

Receptor sequence
>2igqA (length=251) Species: 9606 (Homo sapiens) [Search protein sequence]
ERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMNIDRNI
THLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECN
HACSCWRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYV
GELISDSEADVREEDSYLFDLVYCIDARFYGNVSRFINHHCEPNLVPVRV
FMAHQDLRFPRIAFFSTRLIEAGEQLGFDYGERFWDIKGSCRCGSPKCRH
S
3D structure
PDB2igq Structural biology of human H3K9 methyltransferases
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y1124 Y1211
Catalytic site (residue number reindexed from 1) Y149 Y230
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 A C1031 C1044 C1074 C1078 C56 C69 C99 C103
BS02 ZN A C1037 C1074 C1080 C1084 C62 C99 C105 C109
BS03 ZN A C1031 C1033 C1037 C1042 C56 C58 C62 C67
BS04 ZN A C1172 C1225 C1227 C1232 C191 C241 C243 C248
BS05 SAH A M1105 W1107 Y1142 R1166 F1167 N1169 H1170 Y1211 C1225 R1226 M130 W132 Y167 R185 F186 N188 H189 Y230 C241 R242 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

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Molecular Function
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Cellular Component
External links
PDB RCSB:2igq, PDBe:2igq, PDBj:2igq
PDBsum2igq
PubMed20084102
UniProtQ9H9B1|EHMT1_HUMAN Histone-lysine N-methyltransferase EHMT1 (Gene Name=EHMT1)

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