Calcium in PDB 7w2t: Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose

All present enzymatic activity of Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose:
3.2.1.45;

The structure of Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose, PDB code: 7w2t 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 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	80.377, 124.458, 174.263, 90, 90, 90
R / Rfree (%)	15.3 / 20.3

The binding sites of Calcium atom in the Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose (pdb code 7w2t). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose, PDB code: 7w2t:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose


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 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca907 b:47.0 occ:1.00 OD1 A:ASP579 2.3 31.8 1.0 O A:ILE581 2.4 32.2 1.0 OD1 A:ASP575 2.4 38.9 1.0 OD1 A:ASP583 2.5 40.0 1.0 OD1 A:ASP577 2.8 64.5 1.0 CG A:ASP583 3.1 38.6 1.0 OD2 A:ASP583 3.3 40.0 1.0 CG A:ASP579 3.3 39.6 1.0 CG A:ASP575 3.5 42.1 1.0 CG A:ASP577 3.5 60.3 1.0 C A:ILE581 3.6 32.8 1.0 OD2 A:ASP577 3.8 68.6 1.0 OD2 A:ASP579 3.8 38.0 1.0 CA A:ASP575 4.1 44.4 1.0 N A:ASP583 4.2 31.3 1.0 N A:ASP579 4.2 38.1 1.0 N A:LYS576 4.2 50.0 1.0 N A:ASP577 4.2 53.2 1.0 N A:ILE581 4.2 31.9 1.0 C A:PRO582 4.3 32.1 1.0 CB A:ASP575 4.3 43.1 1.0 CA A:ILE581 4.3 32.1 1.0 OD2 A:ASP575 4.3 38.8 1.0 CB A:ASP583 4.3 37.5 1.0 CB A:ASP579 4.4 36.0 1.0 CB A:ILE581 4.4 30.3 1.0 C A:ASP575 4.4 48.6 1.0 CA A:ASP583 4.5 33.4 1.0 O A:PRO582 4.6 28.1 1.0 N A:PRO582 4.6 34.0 1.0 OG1 A:THR600 4.6 31.3 1.0 CA A:ASP579 4.7 35.9 1.0 CA A:PRO582 4.7 32.3 1.0 CB A:ASP577 4.7 54.1 1.0 N A:ASN578 4.8 48.0 1.0 CA A:ASP577 4.8 52.5 1.0 N A:GLY580 4.9 32.2 1.0 C A:ASP577 4.9 49.4 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of TXGH116 E730Q Mutant From Thermoanaerobacterium Xylanolyticum with Glucose within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca904 b:65.0 occ:1.00 OD1 B:ASP583 2.4 55.3 1.0 O B:ILE581 2.4 47.1 1.0 OD1 B:ASP579 2.5 48.0 1.0 OD1 B:ASP575 2.5 44.3 1.0 O B:HOH1028 2.7 50.1 1.0 OD1 B:ASP577 2.7 67.8 1.0 CG B:ASP579 3.1 51.7 1.0 OD2 B:ASP579 3.3 52.6 1.0 CG B:ASP583 3.4 54.1 1.0 CG B:ASP577 3.5 70.3 1.0 CG B:ASP575 3.5 45.8 1.0 C B:ILE581 3.6 43.9 1.0 OD2 B:ASP577 3.7 82.4 1.0 OD2 B:ASP583 3.8 57.6 1.0 N B:ILE581 4.1 41.8 1.0 N B:ASP579 4.2 54.1 1.0 CB B:ASP579 4.2 51.2 1.0 CA B:ASP575 4.2 47.6 1.0 CA B:ILE581 4.3 44.2 1.0 N B:LYS576 4.3 52.6 1.0 CB B:ASP575 4.3 46.2 1.0 CB B:ILE581 4.3 42.8 1.0 N B:ASP577 4.3 64.2 1.0 N B:ASP583 4.3 43.5 1.0 C B:PRO582 4.3 45.1 1.0 OD2 B:ASP575 4.4 44.3 1.0 CB B:ASP583 4.5 52.4 1.0 OG1 B:THR600 4.5 41.2 1.0 O B:PRO582 4.5 44.9 1.0 CA B:ASP583 4.6 49.2 1.0 C B:ASP575 4.6 49.5 1.0 N B:PRO582 4.7 44.6 1.0 CA B:ASP579 4.7 51.9 1.0 N B:ASN578 4.7 57.9 1.0 CB B:ASP577 4.7 67.4 1.0 N B:GLY580 4.8 44.7 1.0 CA B:ASP577 4.8 62.8 1.0 CA B:PRO582 4.8 44.3 1.0 C B:ASP577 4.9 57.7 1.0 C B:ASP579 5.0 49.0 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