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Atomistry » Magnesium » PDB 1zk3-207d » 1zs9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1zk3-207d » 1zs9 » |
Magnesium in PDB 1zs9: Crystal Structure of Human Enolase-Phosphatase E1Protein crystallography data
The structure of Crystal Structure of Human Enolase-Phosphatase E1, PDB code: 1zs9
was solved by
H.Wang,
H.Pang,
M.Bartlam,
Z.Rao,
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 Crystal Structure of Human Enolase-Phosphatase E1
(pdb code 1zs9). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Human Enolase-Phosphatase E1, PDB code: 1zs9: Jump to Magnesium binding site number: 1; 2; 3; Magnesium binding site 1 out of 3 in 1zs9Go back to Magnesium Binding Sites List in 1zs9
Magnesium binding site 1 out
of 3 in the Crystal Structure of Human Enolase-Phosphatase E1
Mono view Stereo pair view
Magnesium binding site 2 out of 3 in 1zs9Go back to Magnesium Binding Sites List in 1zs9
Magnesium binding site 2 out
of 3 in the Crystal Structure of Human Enolase-Phosphatase E1
Mono view Stereo pair view
Magnesium binding site 3 out of 3 in 1zs9Go back to Magnesium Binding Sites List in 1zs9
Magnesium binding site 3 out
of 3 in the Crystal Structure of Human Enolase-Phosphatase E1
Mono view Stereo pair view
Reference:
H.Wang,
H.Pang,
M.Bartlam,
Z.Rao.
Crystal Structure of Human E1 Enzyme and Its Complex with A Substrate Analog Reveals the Mechanism of Its Phosphatase/Enolase J.Mol.Biol. V. 348 917 2005.
Page generated: Mon Dec 14 07:12:22 2020
ISSN: ISSN 0022-2836 PubMed: 15843022 DOI: 10.1016/J.JMB.2005.01.072 |
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