Structure of PDB 1ozv Chain A Binding Site BS01

Receptor Information
>1ozv Chain A (length=429) 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
EDHAYEVKYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNEN
RHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPY
LRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSAL
AGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELEL
DQLEYYQERRLKDLGLCGENGDILENLYF
Ligand information
Ligand IDLYS
InChIInChI=1S/C6H14N2O2/c7-4-2-1-3-5(8)6(9)10/h5H,1-4,7-8H2,(H,9,10)/p+1/t5-/m0/s1
InChIKeyKDXKERNSBIXSRK-YFKPBYRVSA-O
SMILES
SoftwareSMILES
CACTVS 3.341N[CH](CCCC[NH3+])C(O)=O
ACDLabs 10.04O=C(O)C(N)CCCC[NH3+]
OpenEye OEToolkits 1.5.0C(CC[NH3+])C[C@@H](C(=O)O)N
CACTVS 3.341N[C@@H](CCCC[NH3+])C(O)=O
OpenEye OEToolkits 1.5.0C(CC[NH3+])CC(C(=O)O)N
FormulaC6 H15 N2 O2
NameLYSINE
ChEMBL
DrugBank
ZINC
PDB chain1ozv Chain A Residue 700 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1ozv Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
Resolution2.65 Å
Binding residue
(original residue number in PDB)		R222 F224 R226 Y254 Y287
Binding residue
(residue number reindexed from 1)		R173 F175 R177 Y205 Y229
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=1.44,Ki=36.6mM
Enzymatic activity
Catalytic site (original residue number in PDB) Y287
Catalytic site (residue number reindexed from 1) Y229
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:1ozv, PDBe:1ozv, PDBj:1ozv
PDBsum1ozv
PubMed12819771
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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