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Atomistry » Calcium » PDB 8hhv-8ihw » 8i5s » |
Calcium in PDB 8i5s: Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-FluoroglucosideEnzymatic activity of Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside
All present enzymatic activity of Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside:
3.2.1.21; Protein crystallography data
The structure of Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside, PDB code: 8i5s
was solved by
S.Pengthaisong,
J.R.Ketudat Cairns,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8i5s:
The structure of Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside
(pdb code 8i5s). 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 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside, PDB code: 8i5s: Calcium binding site 1 out of 1 in 8i5sGo back to Calcium Binding Sites List in 8i5s
Calcium binding site 1 out
of 1 in the Crystal Structure of TXGH116 D593N Acid/Base Mutant From Thermoanaerobacterium Xylanolyticum with 2-Deoxy-2-Fluoroglucoside
Mono view Stereo pair view
Reference:
S.Pengthaisong,
B.Piniello,
G.J.Davies,
C.Rovira,
J.R.K.Cairns.
Reaction Mechanism of Glycoside Hydrolase Family 116 Utilizes Perpendicular Protonation Acs Catalysis 5850 2023.
Page generated: Fri Jul 19 09:36:39 2024
ISSN: ESSN 2155-5435 DOI: 10.1021/ACSCATAL.3C00620 |
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