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Chlorine in PDB 5ct9: G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl]

Enzymatic activity of G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl]

All present enzymatic activity of G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl]:
3.1.1.3;

Protein crystallography data

The structure of G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl], PDB code: 5ct9 was solved by E.M.Nordwald, J.G.Plaks, J.R.Snell, M.C.Sousa, J.L.Kaar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.91 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.140, 55.900, 64.410, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 15.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl] (pdb code 5ct9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl], PDB code: 5ct9:

Chlorine binding site 1 out of 1 in 5ct9

Go back to Chlorine Binding Sites List in 5ct9
Chlorine binding site 1 out of 1 in the G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl]


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of G158E/K44E/R57E/Y49E Bacillus Subtilis Lipase A with 5% [Bmim][Cl] within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl201

b:15.1
occ:0.98
H A:HIS156 2.4 7.8 1.0
H A:MET134 2.4 11.2 1.0
H2 A:HOH479 2.9 18.4 1.0
HB2 A:MET134 3.0 16.7 1.0
O A:HOH373 3.1 24.9 1.0
N A:HIS156 3.2 6.5 1.0
O A:HOH479 3.2 15.3 1.0
N A:MET134 3.2 9.3 1.0
HB2 A:HIS156 3.3 8.6 1.0
HG2 A:MET134 3.3 22.4 1.0
HG12 A:ILE135 3.3 18.9 1.0
HA2 A:GLY155 3.3 8.5 1.0
HA A:ASP133 3.4 10.6 1.0
HB3 A:HIS156 3.5 8.6 1.0
H2 A:HOH373 3.6 29.9 1.0
H1 A:HOH373 3.6 29.9 1.0
H1 A:HOH479 3.6 18.4 1.0
CB A:MET134 3.6 13.9 1.0
HA3 A:GLY155 3.7 8.5 1.0
CG A:MET134 3.7 18.6 1.0
CB A:HIS156 3.8 7.1 1.0
HG3 A:MET134 3.8 22.4 1.0
CA A:GLY155 3.9 7.1 1.0
CA A:MET134 4.0 11.7 1.0
C A:GLY155 4.0 6.9 1.0
O A:ALA132 4.1 13.3 1.0
H A:ILE135 4.1 11.1 1.0
CA A:HIS156 4.1 6.7 1.0
CA A:ASP133 4.2 8.8 1.0
C A:ASP133 4.2 8.8 1.0
H2 A:HOH482 4.2 14.9 1.0
CG1 A:ILE135 4.2 15.8 1.0
HG13 A:ILE135 4.4 18.9 1.0
OD1 A:ASP133 4.5 8.4 1.0
N A:ILE135 4.5 9.2 1.0
HB3 A:MET134 4.5 16.7 1.0
H A:ILE157 4.6 9.1 1.0
C A:MET134 4.6 11.3 1.0
O A:HOH482 4.6 12.4 1.0
HD11 A:ILE135 4.6 19.8 1.0
HA A:HIS156 4.7 8.0 1.0
HA A:MET134 4.8 14.1 1.0
CD1 A:ILE135 4.9 16.5 1.0
C A:ALA132 4.9 9.1 1.0
CG A:ASP133 5.0 8.3 1.0

Reference:

E.M.Nordwald, J.G.Plaks, J.R.Snell, M.C.Sousa, J.L.Kaar. Crystallographic Investigation of Imidazolium Ionic Liquid Effects on Enzyme Structure. Chembiochem V. 16 2456 2015.
ISSN: ESSN 1439-7633
PubMed: 26388426
DOI: 10.1002/CBIC.201500398
Page generated: Fri Jul 26 06:15:36 2024

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