Structure of PDB 1ozv Chain C

Receptor sequence

>1ozvC (length=440) Species: 3888 (Pisum sativum)

SLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQ
VPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFG
ILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILP
NKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVT
TEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELAL
DYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYN
RTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCK
AVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQID
GIFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYFQ

3D structure

• PDB: 1ozv Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
• Chain: C
• Resolution: 2.65 Å

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	LYS	C	S221 R222 S225 R226 Y254 Y287	S173 R174 S177 R178 Y206 Y239
BS02	SAH	C	E80 L82 R222 D239 L240 N242 H243 Y287 Y300 F302	E32 L34 R174 D191 L192 N194 H195 Y239 Y252 F254

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:1ozv, PDBe:1ozv, PDBj:1ozv
• PDBsum: 1ozv
• PubMed: 12819771
• UniProt: Q43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)