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Magnesium in PDB 5ded: Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
Enzymatic activity of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
All present enzymatic activity of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp:
2.7.6.5;
2.7.6.5;
Protein crystallography data
The structure of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp, PDB code: 5ded
was solved by
W.Steinchen,
J.S.Schuhmacher,
F.Altegoer,
G.Bange,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 50.57 / 2.94 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 197.869, 113.492, 139.848, 90.00, 127.17, 90.00 |
| R / Rfree (%) | 18.1 / 24.5 |
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
(pdb code 5ded). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp, PDB code: 5ded:
Jump to Magnesium binding site number: 1; 2; 3; 4;
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp, PDB code: 5ded:
Jump to Magnesium binding site number: 1; 2; 3; 4;
Magnesium binding site 1 out of 4 in 5ded
Go back to
Magnesium Binding Sites List in 5ded
Magnesium binding site 1 out
of 4 in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
Mono view
Stereo pair view
Mono view
Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp within 5.0Å range:
|
Magnesium binding site 2 out of 4 in 5ded
Go back to
Magnesium Binding Sites List in 5ded
Magnesium binding site 2 out
of 4 in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
Mono view
Stereo pair view
Mono view
Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp within 5.0Å range:
|
Magnesium binding site 3 out of 4 in 5ded
Go back to
Magnesium Binding Sites List in 5ded
Magnesium binding site 3 out
of 4 in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
Mono view
Stereo pair view
Mono view
Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp within 5.0Å range:
|
Magnesium binding site 4 out of 4 in 5ded
Go back to
Magnesium Binding Sites List in 5ded
Magnesium binding site 4 out
of 4 in the Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp
Mono view
Stereo pair view
Mono view
Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of the Small Alarmone Synthethase 1 From Bacillus Subtilis Bound to Its Product Pppgpp within 5.0Å range:
|
Reference:
W.Steinchen,
J.S.Schuhmacher,
F.Altegoer,
C.D.Fage,
V.Srinivasan,
U.Linne,
M.A.Marahiel,
G.Bange.
Catalytic Mechanism and Allosteric Regulation of An Oligomeric (P)Ppgpp Synthetase By An Alarmone. Proc.Natl.Acad.Sci.Usa V. 112 13348 2015.
ISSN: ESSN 1091-6490
PubMed: 26460002
DOI: 10.1073/PNAS.1505271112
Page generated: Sun Sep 29 02:42:54 2024
ISSN: ESSN 1091-6490
PubMed: 26460002
DOI: 10.1073/PNAS.1505271112
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