Structure of PDB 2h2e Chain B

Receptor sequence

>2h2eB (length=440) Species: 3888 (Pisum sativum)

SLSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQ
VPKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFG
ILPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILP
NKRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVT
TEDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELAL
DYGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYN
RTLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCK
AVREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQID
GIFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYFQ

3D structure

• PDB: 2h2e Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
• Chain: B
• Resolution: 2.6 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	SA8	B	L82 R222 N242 H243 Y287 F302	L34 R174 N194 H195 Y239 F254
BS02	LYS	B	R222 Y287	R174 Y239

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:2h2e, PDBe:2h2e, PDBj:2h2e
• PDBsum: 2h2e
• PubMed: 16682405
• UniProt: Q43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)