Structure of PDB 1mlv Chain A

Receptor sequence

>1mlvA (length=424) Species: 3888 (Pisum sativum)

LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLNLVVVPMADLINHSAGVTTEDH
AYEVYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNENRHAY
TLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPYLRLV
ALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSALAGYH
TTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELELDQLE
YYQERRLKDLGLCGENGDILENLY

3D structure

• PDB: 1mlv Structure and catalytic mechanism of a SET domain protein methyltransferase.
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y287
• Catalytic site (residue number reindexed from 1): Y225
• 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	A	E80 L82 R222 L240 N242 H243 Y287 Y300 F302	E31 L33 R173 L188 N190 H191 Y225 Y238 F240
BS02	EPE	A	S221 R222 F224 S225 R226 D239 L240 I241	S172 R173 F175 S176 R177 D187 L188 I189

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

External links

• PDB: RCSB:1mlv, PDBe:1mlv, PDBj:1mlv
• PDBsum: 1mlv
• PubMed: 12372303
• UniProt: Q43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)