Calcium in PDB 7w2v: Crystal Structure of TXGH116 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose

Enzymatic activity of Crystal Structure of TXGH116 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose

All present enzymatic activity of Crystal Structure of TXGH116 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose:
3.2.1.45;

Protein crystallography data

The structure of Crystal Structure of TXGH116 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose, PDB code: 7w2v 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) 30.00 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 177.444, 54.225, 83.112, 90, 90, 90
R / Rfree (%) 15.3 / 18.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of TXGH116 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose (pdb code 7w2v). 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 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose, PDB code: 7w2v:

Calcium binding site 1 out of 1 in 7w2v

Go back to Calcium Binding Sites List in 7w2v
Calcium binding site 1 out of 1 in the Crystal Structure of TXGH116 R786A 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 R786A Mutant From Thermoanaerobacterium Xylanolyticum with Glucose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca911

b:33.2
occ:1.00
 OD1 A:ASP583 2.3 32.0 1.0
OD1 A:ASP579 2.4 29.0 1.0
O A:ILE581 2.4 26.7 1.0
OD1 A:ASP577 2.4 41.7 1.0
OD1 A:ASP575 2.4 29.1 1.0
O A:HOH1051 2.5 27.1 1.0
CG A:ASP583 3.1 33.6 1.0
CG A:ASP579 3.2 30.7 1.0
OD2 A:ASP583 3.4 38.9 1.0
O A:HOH1202 3.4 45.1 1.0
CG A:ASP575 3.5 27.2 1.0
CG A:ASP577 3.6 43.8 1.0
OD2 A:ASP579 3.6 33.5 1.0
C A:ILE581 3.6 26.9 1.0
CA A:ASP575 4.1 30.9 1.0
OD2 A:ASP577 4.1 44.9 1.0
N A:ASP583 4.1 27.3 1.0
N A:ASP577 4.2 38.9 1.0
N A:LYS576 4.2 37.4 1.0
N A:ILE581 4.2 25.9 1.0
C A:PRO582 4.2 27.3 1.0
CB A:ASP575 4.3 29.3 1.0
N A:ASP579 4.3 34.3 1.0
CA A:ILE581 4.3 25.7 1.0
CB A:ASP583 4.3 30.9 1.0
CB A:ASP579 4.4 33.4 1.0
OD2 A:ASP575 4.4 28.1 1.0
CB A:ILE581 4.4 25.9 1.0
C A:ASP575 4.4 32.2 1.0
CA A:ASP583 4.5 27.0 1.0
OG1 A:THR600 4.5 26.0 1.0
O A:PRO582 4.5 28.3 1.0
N A:PRO582 4.6 27.1 1.0
CA A:PRO582 4.7 27.1 1.0
CB A:ASP577 4.7 40.2 1.0
CA A:ASP579 4.7 33.1 1.0
CA A:ASP577 4.8 40.1 1.0
N A:ASN578 4.8 38.7 1.0
C A:ASP577 4.9 38.4 1.0
N A:GLY580 5.0 29.8 1.0

Reference:

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
Page generated: Tue Apr 4 19:05:55 2023

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