Structure of PDB 2h23 Chain B Binding Site BS02

Receptor Information
>2h23 Chain B (length=440) Species: 3888 (Pisum sativum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQ
VPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFG
ILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILP
NKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVT
TEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELAL
DYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYN
RTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCK
AVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQID
GIFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYFQ
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 B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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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 D239 I241 H252 Y287
Binding residue
(residue number reindexed from 1)		R174 F176 R178 D191 I193 H204 Y239
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y287
Catalytic site (residue number reindexed from 1) Y239
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

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Molecular Function
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Biological Process
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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)

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