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Atomistry » Zinc » PDB 1tbn-1tny » 1tn8 » |
Zinc in PDB 1tn8: Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A ResolutionEnzymatic activity of Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution
All present enzymatic activity of Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution:
2.5.1.58; Protein crystallography data
The structure of Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution, PDB code: 1tn8
was solved by
T.S.Reid,
K.L.Terry,
P.J.Casey,
L.S.Beese,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution
(pdb code 1tn8). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution, PDB code: 1tn8: Zinc binding site 1 out of 1 in 1tn8Go back to Zinc Binding Sites List in 1tn8
Zinc binding site 1 out
of 1 in the Protein Farnesyltransferase Complexed with A H-Ras Peptide Substrate and A Fpp Analog at 2.25A Resolution
Mono view Stereo pair view
Reference:
T.S.Reid,
K.L.Terry,
P.J.Casey,
L.S.Beese.
Crystallographic Analysis of Caax Prenyltransferases Complexed with Substrates Defines Rules of Protein Substrate Selectivity. J.Mol.Biol. V. 343 417 2004.
Page generated: Wed Dec 16 03:04:57 2020
ISSN: ISSN 0022-2836 PubMed: 15451670 DOI: 10.1016/J.JMB.2004.08.056 |
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