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Atomistry » Magnesium » PDB 2xbp-2xnd » 2xbp | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 2xbp-2xnd » 2xbp » |
Magnesium in PDB 2xbp: A Novel Signal Transduction Protein Pii Variant From Synechococcus Elongatus PCC7942 Indicates A Two-Step Process For Nagk Pii Complex FormationProtein crystallography data
The structure of A Novel Signal Transduction Protein Pii Variant From Synechococcus Elongatus PCC7942 Indicates A Two-Step Process For Nagk Pii Complex Formation, PDB code: 2xbp
was solved by
O.Fokina,
V.R.Chellamuthu,
K.Zeth,
K.Forchhammer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2xbp:
The structure of A Novel Signal Transduction Protein Pii Variant From Synechococcus Elongatus PCC7942 Indicates A Two-Step Process For Nagk Pii Complex Formation also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the A Novel Signal Transduction Protein Pii Variant From Synechococcus Elongatus PCC7942 Indicates A Two-Step Process For Nagk Pii Complex Formation
(pdb code 2xbp). 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 A Novel Signal Transduction Protein Pii Variant From Synechococcus Elongatus PCC7942 Indicates A Two-Step Process For Nagk Pii Complex Formation, PDB code: 2xbp: Magnesium binding site 1 out of 1 in 2xbpGo back to Magnesium Binding Sites List in 2xbp
Magnesium binding site 1 out
of 1 in the A Novel Signal Transduction Protein Pii Variant From Synechococcus Elongatus PCC7942 Indicates A Two-Step Process For Nagk Pii Complex Formation
Mono view Stereo pair view
Reference:
O.Fokina,
V.R.Chellamuthu,
K.Zeth,
K.Forchhammer.
A Novel Signal Transduction Protein P(II) Variant From Synechococcus Elongatus Pcc 7942 Indicates A Two-Step Process For Nagk- P(II) Complex Formation. J.Mol.Biol. V. 399 410 2010.
Page generated: Wed Aug 14 07:04:49 2024
ISSN: ISSN 0022-2836 PubMed: 20399792 DOI: 10.1016/J.JMB.2010.04.018 |
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