Structure of PDB 1kyz Chain E

Receptor sequence
>1kyzE (length=361) Species: 3879 (Medicago sativa) [Search protein sequence]
GETQITPTHISDEEANLFAMQLASASVLPMILKSALELDLLEIIAKAGPG
AQISPIEIASQLPTTNPDAPVMLDRMLRLLACYIILTCSVRTQQDGKVQR
LYGLATVAKYLVKNEDGVSISALNLMNQDKVLMESWYHLKDAVLDGGIPF
NKAYGMTAFEYHGTDPRFNKVFNKGMSDHSTITMKKILETYTGFEGLKSL
VDVGGGTGAVINTIVSKYPTIKGINFDLPHVIEDAPSYPGVEHVGGDMFV
SIPKADAVFMKWICHDWSDEHCLKFLKNCYEALPDNGKVIVAECILPVAP
DSSLATKGVVHIDVIMLAHNPGGKERTQKEFEDLAKGAGFQGFKVHCNAF
NTYIMEFLKKV
3D structure
PDB1kyz Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase.
ChainE
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H269 D270 E297 E329
Catalytic site (residue number reindexed from 1) H265 D266 E293 E325
Enzyme Commision number 2.1.1.68: caffeate O-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 SAH E G208 D231 L232 D251 M252 F253 K265 W266 W271 G204 D227 L228 D247 M248 F249 K261 W262 W267
BS02 FER E M130 A162 D270 M320 M126 A158 D266 M316
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008171 O-methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0046983 protein dimerization activity
GO:0047763 caffeate O-methyltransferase activity
Biological Process
GO:0009699 phenylpropanoid biosynthetic process
GO:0009809 lignin biosynthetic process
GO:0032259 methylation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1kyz, PDBe:1kyz, PDBj:1kyz
PDBsum1kyz
PubMed12084826
UniProtP28002|COMT1_MEDSA Caffeic acid 3-O-methyltransferase

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