Structure of PDB 2h2j Chain A Binding Site BS02

Receptor Information
>2h2j Chain A (length=423) 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
AYEYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNENRHAYT
LTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPYLRLVA
LGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSALAGYHT
TIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELELDQLEY
YQERRLKDLGLCGENGDILENLY
Ligand information
Ligand IDMLZ
InChIInChI=1S/C7H16N2O2/c1-9-5-3-2-4-6(8)7(10)11/h6,9H,2-5,8H2,1H3,(H,10,11)/t6-/m0/s1
InChIKeyPQNASZJZHFPQLE-LURJTMIESA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CNCCCCC(C(=O)O)N
OpenEye OEToolkits 1.5.0CNCCCC[C@@H](C(=O)O)N
CACTVS 3.341CNCCCC[CH](N)C(O)=O
CACTVS 3.341CNCCCC[C@H](N)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCCNC
FormulaC7 H16 N2 O2
NameN-METHYL-LYSINE
ChEMBL
DrugBankDB01714
ZINCZINC000001529511
PDB chain2h2j Chain A Residue 900 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2h2j Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		R222 F224 S225 Y287
Binding residue
(residue number reindexed from 1)		R173 F175 S176 Y224
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y287
Catalytic site (residue number reindexed from 1) Y224
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:2h2j, PDBe:2h2j, PDBj:2h2j
PDBsum2h2j
PubMed16682405
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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