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Atomistry » Magnesium » PDB 3rer-3rqx » 3rlf » |
Magnesium in PDB 3rlf: Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to MgamppnpEnzymatic activity of Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp
All present enzymatic activity of Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp:
3.6.3.19; Protein crystallography data
The structure of Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp, PDB code: 3rlf
was solved by
M.L.Oldham,
J.Chen,
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 the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp
(pdb code 3rlf). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp, PDB code: 3rlf: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3rlfGo back to Magnesium Binding Sites List in 3rlf
Magnesium binding site 1 out
of 2 in the Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3rlfGo back to Magnesium Binding Sites List in 3rlf
Magnesium binding site 2 out
of 2 in the Crystal Structure of the Maltose-Binding Protein/Maltose Transporter Complex in An Outward-Facing Conformation Bound to Mgamppnp
Mono view Stereo pair view
Reference:
M.L.Oldham,
J.Chen.
Snapshots of the Maltose Transporter During Atp Hydrolysis. Proc.Natl.Acad.Sci.Usa V. 108 15152 2011.
Page generated: Thu Aug 15 10:31:36 2024
ISSN: ISSN 0027-8424 PubMed: 21825153 DOI: 10.1073/PNAS.1108858108 |
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