Structure of PDB 1p0y Chain B Binding Site BS01

Receptor Information
>1p0y Chain B (length=441) Species: 3888 (Pisum sativum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PSLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVIL
QVPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYF
GILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIIL
PNKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGV
TTEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELA
LDYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFY
NRTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLC
KAVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQI
DGIFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYFQ
Ligand information
Ligand IDSAH
InChIInChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
InChIKeyZJUKTBDSGOFHSH-WFMPWKQPSA-N
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCSC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
CACTVS 3.341N[C@@H](CCSC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
ACDLabs 10.04O=C(O)C(N)CCSCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CSCC[C@@H](C(=O)O)N)O)O)N
FormulaC14 H20 N6 O5 S
NameS-ADENOSYL-L-HOMOCYSTEINE
ChEMBLCHEMBL418052
DrugBankDB01752
ZINCZINC000004228232
PDB chain1p0y 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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PDB1p0y Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
Resolution2.55 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)		E33 L35 S174 R175 D192 L193 N195 H196 Y240 Y253 F255
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) Y287
Catalytic site (residue number reindexed from 1) Y240
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:1p0y, PDBe:1p0y, PDBj:1p0y
PDBsum1p0y
PubMed12819771
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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