Structure of PDB 2h21 Chain C

Receptor sequence
>2h21C (length=438) Species: 3888 (Pisum sativum) [Search protein sequence]
LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVTT
EDHAYEVKGAAGLFSWDYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALD
YGFIEPNENRHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNR
TLPPGLLPYLRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKA
VREACKSALAGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDG
IFEQKELELDQLEYYQERRLKDLGLCGENGDILENLYF
3D structure
PDB2h21 Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.
ChainC
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) 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 SAM C E80 L82 S221 R222 D239 L240 N242 H243 Y287 Y300 F302 E31 L33 S172 R173 D190 L191 N193 H194 Y238 Y251 F253 MOAD: Kd=0.29uM
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2h21, PDBe:2h21, PDBj:2h21
PDBsum2h21
PubMed16682405
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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