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Atomistry » Magnesium » PDB 1v5g-1vq4 » 1vpe | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1v5g-1vq4 » 1vpe » |
Magnesium in PDB 1vpe: Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga MaritimaEnzymatic activity of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima
All present enzymatic activity of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima:
2.7.2.3; Protein crystallography data
The structure of Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima, PDB code: 1vpe
was solved by
G.Auerbach,
R.Huber,
M.Graettinger,
K.Zaiss,
H.Schurig,
R.Jaenicke,
U.Jacob,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima
(pdb code 1vpe). 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 Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima, PDB code: 1vpe: Magnesium binding site 1 out of 1 in 1vpeGo back to![]() ![]()
Magnesium binding site 1 out
of 1 in the Crystallographic Analysis of Phosphoglycerate Kinase From the Hyperthermophilic Bacterium Thermotoga Maritima
![]() Mono view ![]() Stereo pair view
Reference:
G.Auerbach,
R.Huber,
M.Grattinger,
K.Zaiss,
H.Schurig,
R.Jaenicke,
U.Jacob.
Closed Structure of Phosphoglycerate Kinase From Thermotoga Maritima Reveals the Catalytic Mechanism and Determinants of Thermal Stability. Structure V. 5 1475 1997.
Page generated: Tue Aug 13 15:06:41 2024
ISSN: ISSN 0969-2126 PubMed: 9384563 DOI: 10.1016/S0969-2126(97)00297-9 |
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