Structure of PDB 2h2e Chain C

Receptor sequence

>2h2eC (length=438) Species: 3888 (Pisum sativum)

LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVTT
EDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALD
YGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNR
TLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKA
VREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDG
IFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYF

3D structure

• PDB: 2h2e Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
• Chain: C
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y287
• Catalytic site (residue number reindexed from 1): Y238
• 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	C	E80 G81 L82 S221 R222 L240 N242 H243 Y287	E31 G32 L33 S172 R173 L191 N193 H194 Y238
BS02	LYS	C	R222 S225 Y254 Y287	R173 S176 Y205 Y238

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)