Structure of PDB 2h2e Chain B Binding Site BS01

Receptor Information
>2h2e 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 IDSA8
InChIInChI=1S/C15H23N7O5/c1-21(3-2-7(16)15(25)26)4-8-10(23)11(24)14(27-8)22-6-20-9-12(17)18-5-19-13(9)22/h5-8,10-11,14,23-24H,2-4,16H2,1H3,(H,25,26)(H2,17,18,19)/t7-,8+,10+,11+,14+/m0/s1
InChIKeyJISVTSUBJCPLSV-TWBCTODHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CN(CCC(C(=O)O)N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341CN(CC[CH](N)C(O)=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.341CN(CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(O)C(N)CCN(C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0C[N@@](CC[C@@H](C(=O)O)N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
FormulaC15 H23 N7 O5
NameS-5'-AZAMETHIONINE-5'-DEOXYADENOSINE;
5'-[N-[(3S)-3-AMINO-3-CARBOXYPROPYL]-N-METHYLAMINO]-5'-DEOXYADENOSINE
ChEMBLCHEMBL1235825
DrugBankDB03458
ZINC
PDB chain2h2e Chain B Residue 801 [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)		L82 R222 N242 H243 Y287 F302
Binding residue
(residue number reindexed from 1)		L34 R174 N194 H195 Y239 F254
Annotation score3
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: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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