Structure of PDB 2h2j Chain A

Receptor sequence
>2h2jA (length=423) Species: 3888 (Pisum sativum) [Search protein sequence]
LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLNLVVVPMADLINHSAGVTTEDH
AYEYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNENRHAYT
LTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPYLRLVA
LGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSALAGYHT
TIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELELDQLEY
YQERRLKDLGLCGENGDILENLY
3D structure
PDB2h2j Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
ChainA
Resolution2.45 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) Y224
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 SFG A E80 G81 L82 P151 T154 S221 R222 D239 N242 H243 Y287 F302 E31 G32 L33 P102 T105 S172 R173 D187 N190 H191 Y224 F239 MOAD: Kd=4.2uM
PDBbind-CN: -logKd/Ki=5.38,Kd=4.2uM
BS02 MLZ A R222 F224 S225 Y287 R173 F175 S176 Y224
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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Cellular Component
External links
PDB RCSB:2h2j, PDBe:2h2j, PDBj:2h2j
PDBsum2h2j
PubMed16682405
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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