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Atomistry » Aluminium » PDB 1vfx-2x2f » 2ngr » |
Aluminium in PDB 2ngr: Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.Protein crystallography data
The structure of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap., PDB code: 2ngr
was solved by
N.Nassar,
G.Hoffman,
J.Clardy,
R.Cerione,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2ngr:
The structure of Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap. also contains other interesting chemical elements:
Aluminium Binding Sites:
The binding sites of Aluminium atom in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.
(pdb code 2ngr). This binding sites where shown within
5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap., PDB code: 2ngr: Aluminium binding site 1 out of 1 in 2ngrGo back to Aluminium Binding Sites List in 2ngr
Aluminium binding site 1 out
of 1 in the Transition State Complex For Gtp Hydrolysis By CDC42: Comparisons of the High Resolution Structures For CDC42 Bound to the Active and Catalytically Compromised Forms of the CDC42-Gap.
Mono view Stereo pair view
Reference:
N.Nassar,
G.R.Hoffman,
D.Manor,
J.C.Clardy,
R.A.Cerione.
Structures of CDC42 Bound to the Active and Catalytically Compromised Forms of CDC42GAP. Nat.Struct.Biol. V. 5 1047 1998.
Page generated: Sat Dec 12 01:31:46 2020
ISSN: ISSN 1072-8368 PubMed: 9846874 DOI: 10.1038/4156 |
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