(S)-8-oxocitronellyl enol synthase / monoterpenoid biosynthetic process / oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor / protein homodimerization activity / identical protein binding / cytosol Similarity search - Function
Mass: 41771.969 Da / Num. of mol.: 1 / Fragment: RESIDUES 23-388 Source method: isolated from a genetically manipulated source Details: The crystallised protein contained residues 23-388 of the wild-type amino acid sequence. The sequence differed from database entry K7WDL7 by an Asp to Asn change at position 87. The N- ...Details: The crystallised protein contained residues 23-388 of the wild-type amino acid sequence. The sequence differed from database entry K7WDL7 by an Asp to Asn change at position 87. The N-terminus retained two residues from the nickel affinity cleavage site. The C-terminus had an additional three vector-derived residues. Source: (gene. exp.) Catharanthus roseus (Madagascar periwinkle) Plasmid: pOPIN-F / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Rosetta 2 / References: UniProt: K7WDL7, EC: 1.3.1.99
Resolution: 1.9→70.6 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.944 / WRfactor Rfree: 0.1783 / WRfactor Rwork: 0.1518 / FOM work R set: 0.8446 / SU B: 6.991 / SU ML: 0.107 / SU R Cruickshank DPI: 0.1447 / SU Rfree: 0.1307 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.145 / ESU R Free: 0.131 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2088
1605
5 %
RANDOM
Rwork
0.1761
-
-
-
obs
0.1777
30404
99.95 %
-
Solvent computation
Ion probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1 Å / Solvent model: MASK
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