Structure of PDB 1ozv Chain A

Receptor sequence
>1ozvA (length=429) Species: 3888 (Pisum sativum) [Search protein sequence]
LSPAVQTFWKWLQEEGVITAKTPVKASVVTEGLGLVALKDISRNDVILQV
PKRLWINPDAVAASEIGRVCSELKPWLSVILFLIRERSREDSVWKHYFGI
LPQETDSTIYWSEEELQELQGSQLLKTTVSVKEYVKNECLKLEQEIILPN
KRLFPDPVTLDDFFWAFGILRSRAFSRLRNENLVVVPMADLINHSAGVTT
EDHAYEVKYLFSLKSPLSVKAGEQVYIQYDLNKSNAELALDYGFIEPNEN
RHAYTLTLEISESDPFFDDKLDVAESNGFAQTAYFDIFYNRTLPPGLLPY
LRLVALGGTDAFLLESLFRDTIWGHLELSVSRDNEELLCKAVREACKSAL
AGYHTTIEQDRELKEGNLDSRLAIAVGIREGEKMVLQQIDGIFEQKELEL
DQLEYYQERRLKDLGLCGENGDILENLYF
3D structure
PDB1ozv Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
ChainA
Resolution2.65 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) Y229
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 A R222 F224 R226 Y254 Y287 R173 F175 R177 Y205 Y229 PDBbind-CN: -logKd/Ki=1.44,Ki=36.6mM
BS02 SAH A E80 G81 L82 P151 S221 R222 D239 N242 H243 Y287 Y300 F302 E31 G32 L33 P102 S172 R173 D190 N193 H194 Y229 Y242 F244
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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Cellular Component
External links
PDB RCSB:1ozv, PDBe:1ozv, PDBj:1ozv
PDBsum1ozv
PubMed12819771
UniProtQ43088|RBCMT_PEA Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic (Gene Name=RBCMT)

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