HYDROLASE / LIPID SYNTHESIS / LIPID A BIOSYNTHESIS
Function / homology
Function and homology information
UDP-3-O-acyl-N-acetylglucosamine deacetylase / UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity / UDP-3-O-acyl-N-acetylglucosamine deacetylase activity / lipid A biosynthetic process / metal ion binding Similarity search - Function
SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
Mass: 18.015 Da / Num. of mol.: 488 / Source method: isolated from a natural source / Formula: H2O
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Details
Compound details
ENGINEERED RESIDUE IN CHAIN A, CYS 181 TO ALA ENGINEERED RESIDUE IN CHAIN B, CYS 181 TO ALA
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.69 Å3/Da / Density % sol: 53.9 %
Crystal grow
Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: CRYSTALS OF LPXC WERE GROWN BY HANGING VAPOR DIFFUSION AT 20 DEG C USING 1 UL OF PROTEIN (184 UM) AND 1 UL OF A RESERVOIR SOLUTION CONTAINING 8% PEG 6000, 100 MM TRIS, PH 8.5, AND 300 MM NACL.
Resolution: 2.2→50.9 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.907 / SU B: 4.662 / SU ML: 0.122 / Cross valid method: THROUGHOUT / ESU R: 0.216 / ESU R Free: 0.19 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 269-271 ARE DISORDERED IN BOTH CHAINS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.225
1836
5 %
RANDOM
Rwork
0.168
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obs
0.171
34736
98.9 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK