Structure of PDB 2h23 Chain A Binding Site BS02

Receptor Information
>2h23 Chain A (length=424) Species: 3888 (Pisum sativum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLNLVVVPMADLINHSAGVTTEDH
AYEVYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNENRHAY
TLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPYLRLV
ALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSALAGYH
TTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELELDQLE
YYQERRLKDLGLCGENGDILENLY
Ligand information
Ligand IDM3L
InChIInChI=1S/C9H20N2O2/c1-11(2,3)7-5-4-6-8(10)9(12)13/h8H,4-7,10H2,1-3H3/p+1/t8-/m0/s1
InChIKeyMXNRLFUSFKVQSK-QMMMGPOBSA-O
SMILES
SoftwareSMILES
CACTVS 3.341C[N+](C)(C)CCCC[C@H](N)C(O)=O
OpenEye OEToolkits 1.5.0C[N+](C)(C)CCCC[C@@H](C(=O)O)N
OpenEye OEToolkits 1.5.0C[N+](C)(C)CCCCC(C(=O)O)N
CACTVS 3.341C[N+](C)(C)CCCC[CH](N)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCC[N+](C)(C)C
FormulaC9 H21 N2 O2
NameN-TRIMETHYLLYSINE
ChEMBLCHEMBL1234168
DrugBankDB03977
ZINCZINC000001529747
PDB chain2h23 Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2h23 Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		R222 F224 R226 I241 Y287 Y300
Binding residue
(residue number reindexed from 1)		R173 F175 R177 I189 Y225 Y238
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y287
Catalytic site (residue number reindexed from 1) Y225
Enzyme Commision number 2.1.1.127: [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase.
2.1.1.259: [fructose-bisphosphate aldolase]-lysine N-methyltransferase.
Gene Ontology
Molecular Function
GO:0016279 protein-lysine N-methyltransferase activity
GO:0030785 [ribulose-bisphosphate carboxylase]-lysine N-methyltransferase activity
Biological Process
GO:0018022 peptidyl-lysine methylation
Cellular Component
GO:0009507 chloroplast

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2h23, PDBe:2h23, PDBj:2h23
PDBsum2h23
PubMed16682405
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

[Back to BioLiP]