Structure of PDB 6yjw Chain A

Receptor sequence
>6yjwA (length=353) Species: 3747 (Fragaria x ananassa) [Search protein sequence]
AVSDEEANLFAMQLASASVLPMVLKAAIELDLLEIMAKAGPGSFLSPSDL
ASQLPTKNPEAPVMLDRMLRLLASYSILTCSLRTLPDGKVERLYCLGPVC
KFLTKNEDGVSIAALCLMNQDKVLVESWYHLKDAVLDGGIPFNKAYGMTA
FDYHGTDPRFNKVFNKGMADHSTITMKKILETYKGFEGLKSIVDVGGGTG
AVVNMIVSKYPSIKGINFDLPHVIEDAPQYPGVQHVGGDMFVSVPKGNAI
FMKWICHDWSDEHCIKFLKNCYAALPDDGKVILAECILPVAPDTSLATKG
VVHMDVIMLAHNPGGKERTEQEFEALAKGSGFQGIRVCCDAFNTYVIEFL
KKI
3D structure
PDB6yjw Proline/alanine-rich sequence (PAS) polypeptides as an alternative to PEG precipitants for protein crystallization.
ChainA
Resolution2.1 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 A F163 M180 S184 G208 D231 L232 D251 M252 K265 I267 F151 M168 S172 G196 D219 L220 D239 M240 K253 I255
BS02 EDO A K37 D133 K134 K25 D121 K122
BS03 EDO A R79 R82 R67 R70
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
Biological Process
GO:0009809 lignin biosynthetic process
GO:0032259 methylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6yjw, PDBe:6yjw, PDBj:6yjw
PDBsum6yjw
PubMed32627748
UniProtQ9M602

[Back to BioLiP]