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Chlorine in PDB 5ct5: Wild-Type Bacillus Subtilis Lipase A with 10% [Bmim][Cl]

Protein crystallography data

The structure of Wild-Type Bacillus Subtilis Lipase A with 10% [Bmim][Cl], PDB code: 5ct5 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) 41.39 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.270, 82.780, 95.500, 90.00, 90.00, 90.00
R / Rfree (%) 12.9 / 17.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Wild-Type Bacillus Subtilis Lipase A with 10% [Bmim][Cl] (pdb code 5ct5). 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 Wild-Type Bacillus Subtilis Lipase A with 10% [Bmim][Cl], PDB code: 5ct5:

Chlorine binding site 1 out of 1 in 5ct5

Go back to Chlorine Binding Sites List in 5ct5
Chlorine binding site 1 out of 1 in the Wild-Type Bacillus Subtilis Lipase A with 10% [Bmim][Cl]


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Wild-Type Bacillus Subtilis Lipase A with 10% [Bmim][Cl] within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl203

b:15.0
occ:1.00
H A:HIS156 2.3 12.8 1.0
H2 A:HOH425 2.4 19.5 1.0
H1 A:HOH305 2.5 30.4 1.0
H A:MET134 2.5 13.7 1.0
H2 A:HOH478 2.8 29.8 1.0
O A:HOH305 3.0 25.3 1.0
HB2 A:MET134 3.0 20.2 1.0
O A:HOH425 3.1 16.2 1.0
O A:HOH478 3.1 24.8 1.0
HG3 A:MET134 3.1 22.0 1.0
HB2 A:HIS156 3.1 11.3 1.0
N A:HIS156 3.2 10.6 1.0
HG12 A:ILE135 3.2 17.7 1.0
N A:MET134 3.3 11.4 1.0
HA A:ASP133 3.5 12.8 1.0
HA2 A:GLY155 3.5 13.4 1.0
HE1 A:MET134 3.5 35.2 1.0
H1 A:HOH425 3.5 19.5 1.0
HB3 A:HIS156 3.6 11.3 1.0
HA3 A:GLY155 3.7 13.4 1.0
CB A:MET134 3.7 16.9 1.0
CB A:HIS156 3.7 9.4 1.0
HE3 A:MET134 3.7 35.2 1.0
H2 A:HOH305 3.8 30.4 1.0
CG A:MET134 3.8 18.3 1.0
CA A:GLY155 3.9 11.1 1.0
H2 A:HOH426 3.9 20.8 1.0
H1 A:HOH478 3.9 29.8 1.0
CA A:MET134 4.0 13.7 1.0
C A:GLY155 4.0 11.4 1.0
CE A:MET134 4.0 29.4 1.0
H A:ILE135 4.0 14.7 1.0
CA A:HIS156 4.1 10.4 1.0
O A:ALA132 4.1 10.7 1.0
CG1 A:ILE135 4.1 14.8 1.0
CA A:ASP133 4.3 10.7 1.0
C A:ASP133 4.3 11.0 1.0
HG13 A:ILE135 4.4 17.7 1.0
N A:ILE135 4.4 12.3 1.0
H A:ILE157 4.5 14.5 1.0
OD1 A:ASP133 4.5 9.7 1.0
C A:MET134 4.5 13.7 1.0
HB3 A:MET134 4.6 20.2 1.0
HG2 A:MET134 4.6 22.0 1.0
H2 A:HOH477 4.6 39.5 1.0
HA A:HIS156 4.7 12.4 1.0
HD11 A:ILE135 4.7 21.8 1.0
SD A:MET134 4.7 29.0 1.0
O A:HOH426 4.7 17.3 1.0
HB A:ILE135 4.8 16.6 1.0
H1 A:HOH426 4.9 20.8 1.0
HE2 A:MET134 4.9 35.2 1.0
HA A:MET134 4.9 16.4 1.0
CD1 A:ILE135 4.9 18.1 1.0
HD13 A:ILE135 5.0 21.8 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 06:15:17 2024

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