Structure of PDB 2h21 Chain C Binding Site BS01

Receptor Information
>2h21 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 IDSAM
InChIInChI=1S/C15H22N6O5S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25)/t7-,8+,10+,11+,14+,27-/m0/s1
InChIKeyMEFKEPWMEQBLKI-FCKMPRQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341C[S@@+](CC[C@H](N)C([O-])=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S+](CCC(C(=O)[O-])N)CC1C(C(C(O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.341C[S+](CC[CH](N)C([O-])=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0C[S@@+](CC[C@@H](C(=O)[O-])N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
ACDLabs 10.04[O-]C(=O)C(N)CC[S+](C)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H22 N6 O5 S
NameS-ADENOSYLMETHIONINE
ChEMBLCHEMBL1235831
DrugBank
ZINC
PDB chain2h21 Chain C Residue 803 [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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PDB2h21 Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
Resolution2.45 Å
Binding residue
(original residue number in PDB)		E80 L82 S221 R222 D239 L240 N242 H243 Y287 Y300 F302
Binding residue
(residue number reindexed from 1)		E31 L33 S172 R173 D190 L191 N193 H194 Y238 Y251 F253
Annotation score5
Binding affinityMOAD: Kd=0.29uM
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:2h21, PDBe:2h21, PDBj:2h21
PDBsum2h21
PubMed16682405
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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