Calcium in PDB 7w2x: Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum

All present enzymatic activity of Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum:
3.2.1.45;

The structure of Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum, PDB code: 7w2x was solved by M.Huang, S.Pengthaisong, R.Charoenwattanasatien, J.Jitonnom, J.R.Ketudatcairns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.01 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	176.755, 54.254, 83.035, 90, 90, 90
R / Rfree (%)	14.7 / 18.1

The binding sites of Calcium atom in the Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum (pdb code 7w2x). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum, PDB code: 7w2x:

Calcium binding site 1 out of 1 in the Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of TXGH116 R786K Mutant From Thermoanaerobacterium Xylanolyticum within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca912 b:33.3 occ:1.00 O A:ILE581 2.3 23.6 1.0 OD1 A:ASP583 2.3 28.0 1.0 OD1 A:ASP579 2.4 26.7 1.0 OD1 A:ASP577 2.4 36.9 1.0 OD1 A:ASP575 2.4 27.1 1.0 O A:HOH1081 2.5 26.1 1.0 CG A:ASP583 3.1 28.9 1.0 CG A:ASP579 3.2 27.5 1.0 CG A:ASP575 3.4 25.3 1.0 CG A:ASP577 3.5 40.3 1.0 OD2 A:ASP583 3.5 33.2 1.0 C A:ILE581 3.5 23.4 1.0 OD2 A:ASP579 3.6 27.9 1.0 O A:HOH1012 3.6 42.7 1.0 CA A:ASP575 3.9 26.2 1.0 OD2 A:ASP577 4.0 45.9 1.0 N A:ILE581 4.0 22.4 1.0 N A:LYS576 4.1 30.9 0.5 CB A:ASP575 4.1 26.4 1.0 N A:LYS576 4.1 30.6 0.5 N A:ASP583 4.1 23.9 1.0 N A:ASP577 4.1 34.4 1.0 CA A:ILE581 4.2 22.7 1.0 C A:PRO582 4.2 23.4 1.0 CB A:ILE581 4.3 21.9 1.0 OD2 A:ASP575 4.3 25.7 1.0 N A:ASP579 4.3 31.8 1.0 C A:ASP575 4.3 28.6 1.0 CB A:ASP583 4.3 27.3 1.0 CB A:ASP579 4.4 28.2 1.0 O A:PRO582 4.4 24.5 1.0 CA A:ASP583 4.5 24.1 1.0 OG1 A:THR600 4.5 23.5 1.0 N A:PRO582 4.5 23.1 1.0 CB A:ASP577 4.6 39.0 1.0 CA A:PRO582 4.6 23.6 1.0 CA A:ASP577 4.8 35.5 1.0 CA A:ASP579 4.8 28.9 1.0 N A:ASN578 4.8 33.6 1.0 N A:GLY580 4.8 26.1 1.0 C A:ASP577 4.9 34.4 1.0 C A:ASP579 5.0 27.0 1.0

M.Huang, S.Pengthaisong, R.Charoenwattanasatien, N.Thinkumrob, J.Jitonnom, J.R.Ketudat Cairns. Systematic Functional and Computational Analysis of Glucose-Binding Residues in Glycoside Hydrolase Family GH116. Catalysts V. 12 2022.
ISSN: ESSN 2073-4344
DOI: 10.3390/CATAL12030343