Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
C9M 2-methoxy-4-[(1e)-3-methoxyprop-1-en-1-yl]phenol
GOL Glycerol
N7I 4-[(1e)-3-hydroxyprop-1-en-1-yl]-2-methoxyphenol
SAH S-adenosyl-L-homocysteine
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 4EVI   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum in Complex with Coniferyl Alcohol 9-Methyl Ether and S -Adenosyl-L-Homocysteine
Release Data : 2013-05-01
Compound :
mol_id molecule chains synonym
1 Coniferyl alcohol 9-O-methyltransferase A,B S-adenosyl-L-methionine-dependent coniferyl alcohol 9-O-methyltransferase
Source :
mol_id organism_scientific expression_system
1 Linum nodiflorum  (taxid:407264) Escherichia coli  (taxid:469008)
gene: CA9OMT
expression_system_strain: BL21(DE3)pLysS
expression_system_vector_type: PLASMID
expression_system_plasmid: pet15b
Authors : Wolters, S., Heine, A., Petersen, M.
Keywords : Rossmann fold, Dimer, small molecule O-methyltransferase, TRANSFERASE, S-Adenosyl-L-methionine, coniferyl alcohol, S -Adenosyl-L-homocysteine
Exp. method : X-RAY DIFFRACTION ( 2.0150 Å )
Citation :

Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.

Wolters, S.,Neeb, M.,Berim, A.  et al.
(2013)  Acta Crystallogr.,Sect.D  69 : 888 - 900

PubMed: 23633600
DOI: 10.1107/S0907444913002874

Chain : A, B
UniProt : A6XNE6 (A6XNE6_9ROSI)
Reaction : -