Structure of PDB 1mlv Chain B

Receptor sequence
>1mlvB (length=440) Species: 3888 (Pisum sativum) [Search protein sequence]
SLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQ
VPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFG
ILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILP
NKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVT
TEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELAL
DYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYN
RTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCK
AVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQID
GIFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYFQ
3D structure
PDB1mlv Structure and catalytic mechanism of a SET domain protein methyltransferase.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SAH B E80 G81 L82 R222 D239 N242 H243 Y287 Y300 F302 E32 G33 L34 R174 D191 N194 H195 Y239 Y252 F254
BS02 EPE B S221 R222 F224 S225 R226 D239 I241 H252 Y287 Y300 S173 R174 F176 S177 R178 D191 I193 H204 Y239 Y252
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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