Structure of PDB 1mlv Chain B Binding Site BS02

Receptor Information
>1mlv 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 IDEPE
InChIInChI=1S/C8H18N2O4S/c11-7-5-9-1-3-10(4-2-9)6-8-15(12,13)14/h11H,1-8H2,(H,12,13,14)
InChIKeyJKMHFZQWWAIEOD-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=S(=O)(O)CCN1CCN(CCO)CC1
OpenEye OEToolkits 1.5.0C1CN(CCN1CCO)CCS(=O)(=O)O
CACTVS 3.341OCCN1CCN(CC1)CC[S](O)(=O)=O
FormulaC8 H18 N2 O4 S
Name4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID;
HEPES
ChEMBLCHEMBL1232545
DrugBankDB16872
ZINCZINC000019203136
PDB chain1mlv 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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PDB1mlv Structure and catalytic mechanism of a SET domain protein methyltransferase.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		S221 R222 F224 S225 R226 D239 I241 H252 Y287 Y300
Binding residue
(residue number reindexed from 1)		S173 R174 F176 S177 R178 D191 I193 H204 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:1mlv, PDBe:1mlv, PDBj:1mlv
PDBsum1mlv
PubMed12372303
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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