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Atomistry » Magnesium » PDB 3abl-3aln » 3ahg » |
Magnesium in PDB 3ahg: H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine DiphosphateEnzymatic activity of H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate
All present enzymatic activity of H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate:
4.1.2.22; Protein crystallography data
The structure of H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate, PDB code: 3ahg
was solved by
R.Suzuki,
T.Katayama,
B.-J.Kim,
T.Wakagi,
H.Shoun,
H.Ashida,
K.Yamamoto,
S.Fushinobu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3ahg:
The structure of H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate
(pdb code 3ahg). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate, PDB code: 3ahg: Magnesium binding site 1 out of 1 in 3ahgGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the H64A Mutant of Phosphoketolase From Bifidobacterium Breve Complexed with A Tricyclic Ring Form of Thiamine Diphosphate
![]() Mono view ![]() Stereo pair view
Reference:
R.Suzuki,
T.Katayama,
B.-J.Kim,
T.Wakagi,
H.Shoun,
H.Ashida,
K.Yamamoto,
S.Fushinobu.
Crystal Structures of Phosphoketolase: Thiamine Diphosphate-Dependent Dehydration Mechanism J.Biol.Chem. V. 285 34279 2010.
Page generated: Wed Aug 14 08:36:15 2024
ISSN: ISSN 0021-9258 PubMed: 20739284 DOI: 10.1074/JBC.M110.156281 |
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