Structure of PDB 1p0y Chain C Binding Site BS02

Receptor Information
>1p0y Chain C (length=439) 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
GIFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYF
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 chain1p0y Chain C Residue 902 [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)		R222 F224 S225 D239 Y254 Y287 Y300
Binding residue
(residue number reindexed from 1)		R174 F176 S177 D191 Y206 Y239 Y252
Annotation score1
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: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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