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Atomistry » Magnesium » PDB 1z6n-1zk2 » 1zbd | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1z6n-1zk2 » 1zbd » |
Magnesium in PDB 1zbd: Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3AProtein crystallography data
The structure of Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3A, PDB code: 1zbd
was solved by
C.Ostermeier,
A.T.Brunger,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1zbd:
The structure of Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3A also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3A
(pdb code 1zbd). 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 Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3A, PDB code: 1zbd: Magnesium binding site 1 out of 1 in 1zbdGo back to Magnesium Binding Sites List in 1zbd
Magnesium binding site 1 out
of 1 in the Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3A
Mono view Stereo pair view
Reference:
C.Ostermeier,
A.T.Brunger.
Structural Basis of Rab Effector Specificity: Crystal Structure of the Small G Protein RAB3A Complexed with the Effector Domain of Rabphilin-3A. Cell(Cambridge,Mass.) V. 96 363 1999.
Page generated: Mon Dec 14 07:11:38 2020
ISSN: ISSN 0092-8674 PubMed: 10025402 DOI: 10.1016/S0092-8674(00)80549-8 |
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