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Atomistry » Magnesium » PDB 1gq9-1h7q » 1gua | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1gq9-1h7q » 1gua » |
Magnesium in PDB 1gua: Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131Protein crystallography data
The structure of Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131, PDB code: 1gua
was solved by
N.Nassar,
A.Wittinghofer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1gua:
The structure of Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131 also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131
(pdb code 1gua). 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 Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131, PDB code: 1gua: Magnesium binding site 1 out of 1 in 1guaGo back to Magnesium Binding Sites List in 1gua
Magnesium binding site 1 out
of 1 in the Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131
Mono view Stereo pair view
Reference:
N.Nassar,
G.Horn,
C.Herrmann,
C.Block,
R.Janknecht,
A.Wittinghofer.
Ras/Rap Effector Specificity Determined By Charge Reversal. Nat.Struct.Biol. V. 3 723 1996.
Page generated: Mon Dec 14 05:58:23 2020
ISSN: ISSN 1072-8368 PubMed: 8756332 DOI: 10.1038/NSB0896-723 |
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