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Chlorine in PDB 9gci: The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution

Enzymatic activity of The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution

All present enzymatic activity of The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution:
3.2.1.21;

Protein crystallography data

The structure of The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution, PDB code: 9gci was solved by E.D.Chrysina, A.I.Sotiropoulou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.44 / 1.47
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 68.443, 98.718, 80.493, 90, 97.49, 90
R / Rfree (%) 15.3 / 17.4

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution (pdb code 9gci). 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 The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution, PDB code: 9gci:

Chlorine binding site 1 out of 1 in 9gci

Go back to Chlorine Binding Sites List in 9gci
Chlorine binding site 1 out of 1 in the The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Crystal Structure of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus Determined at 1.47 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl512

b:13.9
occ:1.00
 HZ2 A:LYS152 2.2 14.4 1.0
NZ A:LYS152 3.1 14.6 1.0
O A:HOH845 3.1 15.0 1.0
HD2 A:LYS152 3.2 12.8 1.0
HG12 A:ILE210 3.3 14.9 1.0
HE3 A:LYS152 3.4 13.7 1.0
HZ3 A:LYS152 3.4 14.4 1.0
HA A:ILE210 3.5 13.6 1.0
HG21 A:ILE210 3.5 14.2 1.0
CE A:LYS152 3.6 13.8 1.0
HZ1 A:LYS152 3.6 14.4 1.0
CD A:LYS152 3.9 12.7 1.0
CG1 A:ILE210 4.2 15.0 1.0
H A:ASP211 4.3 14.1 1.0
HD3 A:LYS152 4.3 12.8 1.0
CA A:ILE210 4.4 13.5 1.0
CG2 A:ILE210 4.4 14.3 1.0
HE2 A:LYS152 4.5 13.7 1.0
CB A:ILE210 4.5 14.1 1.0
O A:HOH927 4.7 23.8 1.0
HG13 A:ILE210 4.7 14.9 1.0
HG23 A:ILE210 4.9 14.2 1.0
O A:HOH998 4.9 16.2 1.0
O A:ASN209 5.0 14.2 1.0
HD11 A:ILE210 5.0 15.5 1.0

Reference:

A.I.Sotiropoulou, D.G.Hatzinikolaou, E.D.Chrysina. Structural Studies of Beta-Glucosidase From the Thermophilic Bacterium Caldicellulosiruptor Saccharolyticus. Acta Crystallogr D Struct V. 80 733 2024BIOL.
ISSN: ISSN 2059-7983
PubMed: 39361356
DOI: 10.1107/S2059798324009252
Page generated: Thu Oct 31 18:12:31 2024

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