Oxidoreductases; Acting on the CH-OH group of donors; With oxygen as acceptor / : / fatty acid alpha-oxidation / L-lactate dehydrogenase activity / peroxisome / FMN binding / metal ion binding / plasma membrane Similarity search - Function
L-lactate oxidase / Alpha-hydroxy acid dehydrogenase, FMN-dependent / FMN-dependent alpha-hydroxy acid dehydrogenase, active site / FMN hydroxy acid dehydrogenase domain / FMN-dependent alpha-hydroxy acid dehydrogenases active site. / FMN-dependent alpha-hydroxy acid dehydrogenase domain profile. / FMN-dependent dehydrogenase / FMN-dependent dehydrogenase / Aldolase class I / Aldolase-type TIM barrel ...L-lactate oxidase / Alpha-hydroxy acid dehydrogenase, FMN-dependent / FMN-dependent alpha-hydroxy acid dehydrogenase, active site / FMN hydroxy acid dehydrogenase domain / FMN-dependent alpha-hydroxy acid dehydrogenases active site. / FMN-dependent alpha-hydroxy acid dehydrogenase domain profile. / FMN-dependent dehydrogenase / FMN-dependent dehydrogenase / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta Similarity search - Domain/homology
Mass: 40832.711 Da / Num. of mol.: 8 / Mutation: T102A, S163G, Y215F, G232A, R255A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aerococcus viridans (bacteria) / Production host: Escherichia coli (E. coli) / Strain (production host): DE3 References: UniProt: Q44467, Oxidoreductases; Acting on the CH-OH group of donors; With oxygen as acceptor
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97946 Å / Relative weight: 1
Reflection
Resolution: 2.6→40 Å / Num. obs: 87748 / % possible obs: 99.3 % / Redundancy: 3.75 % / Rmerge(I) obs: 0.077 / Net I/σ(I): 14.7
Reflection shell
Resolution: 2.6→2.74 Å / Redundancy: 3.73 % / Rmerge(I) obs: 0.323 / Mean I/σ(I) obs: 4.8 / % possible all: 96.8
-
Processing
Software
Name
Version
Classification
REFMAC
5.8.0049
refinement
XDS
datareduction
SCALA
datascaling
PHASER
phasing
Refinement
Resolution: 2.6→39.75 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.905 / SU B: 11.711 / SU ML: 0.245 / Cross valid method: THROUGHOUT / ESU R Free: 0.336 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.24596
2637
3 %
RANDOM
Rwork
0.18191
-
-
-
obs
0.18382
85084
99.28 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK