Chlorine in PDB 5ncx: Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor

Enzymatic activity of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor

All present enzymatic activity of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor:
3.2.1.45;

Protein crystallography data

The structure of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor, PDB code: 5ncx was solved by G.J.Davies, I.Z.Breen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.73 / 1.70
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 53.621, 83.295, 177.480, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 18.4

Other elements in 5ncx:

The structure of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor (pdb code 5ncx). 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 Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor, PDB code: 5ncx:

Chlorine binding site 1 out of 1 in 5ncx

Go back to Chlorine Binding Sites List in 5ncx
Chlorine binding site 1 out of 1 in the Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Thermoanaerobacterium Xylolyticum GH116 Beta- Glucosidase with An Covalent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl905

b:53.6
occ:1.00
NZ A:LYS708 3.6 36.0 1.0
OH A:TYR757 3.9 27.8 1.0
CE A:LYS761 3.9 34.2 1.0
CE2 A:TYR757 4.0 25.6 1.0
CE A:LYS708 4.2 34.8 1.0
CZ A:TYR757 4.4 24.3 1.0
CD A:LYS708 4.5 32.1 1.0
CD A:LYS761 4.6 30.5 1.0

Reference:

D.Lahav, B.Liu, R.J.B.H.N.Van Den Berg, A.M.C.H.Van Den Nieuwendijk, T.Wennekes, A.T.Ghisaidoobe, I.Breen, M.J.Ferraz, C.L.Kuo, L.Wu, P.P.Geurink, H.Ovaa, G.A.Van Der Marel, M.Van Der Stelt, R.G.Boot, G.J.Davies, J.M.F.G.Aerts, H.S.Overkleeft. A Fluorescence Polarization Activity-Based Protein Profiling Assay in the Discovery of Potent, Selective Inhibitors For Human Nonlysosomal Glucosylceramidase. J. Am. Chem. Soc. V. 139 14192 2017.
ISSN: ESSN 1520-5126
PubMed: 28937220
DOI: 10.1021/JACS.7B07352
Page generated: Sat Dec 12 12:09:16 2020

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