Structure of PDB 2h2e Chain C Binding Site BS02

Receptor Information
>2h2e Chain C (length=438) Species: 3888 (Pisum sativum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVTT
EDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALD
YGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNR
TLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKA
VREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDG
IFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYF
Ligand information
Ligand IDLYS
InChIInChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/p+1/t5-/m0/s1
InChIKeyKDXKERNSBIXSRK-YFKPBYRVSA-O
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCCC[NH3+])C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCC[NH3+]
OpenEye OEToolkits 1.5.0C(CC[NH3+])C[C@@H](C(=O)O)N
CACTVS 3.341N[C@@H](CCCC[NH3+])C(O)=O
OpenEye OEToolkits 1.5.0C(CC[NH3+])CC(C(=O)O)N
FormulaC6 H15 N2 O2
NameLYSINE
ChEMBL
DrugBank
ZINC
PDB chain2h2e Chain C Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2h2e Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		R222 S225 Y254 Y287
Binding residue
(residue number reindexed from 1)		R173 S176 Y205 Y238
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y287
Catalytic site (residue number reindexed from 1) Y238
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:2h2e, PDBe:2h2e, PDBj:2h2e
PDBsum2h2e
PubMed16682405
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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