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Atomistry » Zinc » PDB 1rrm-1sdy » 1sa5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1rrm-1sdy » 1sa5 » |
Zinc in PDB 1sa5: Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662Enzymatic activity of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662
All present enzymatic activity of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662:
2.5.1.58; 2.5.1.59; Protein crystallography data
The structure of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662, PDB code: 1sa5
was solved by
T.S.Reid,
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 Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662
(pdb code 1sa5). 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 Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662, PDB code: 1sa5: Zinc binding site 1 out of 1 in 1sa5Go back to![]() ![]()
Zinc binding site 1 out
of 1 in the Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662
![]() Mono view ![]() Stereo pair view
Reference:
T.S.Reid,
L.S.Beese.
Crystal Structures of the Anticancer Clinical Candidates R115777 (Tipifarnib) and Bms-214662 Complexed with Protein Farnesyltransferase Suggest A Mechanism of Fti Selectivity. Biochemistry V. 43 6877 2004.
Page generated: Wed Oct 16 18:47:06 2024
ISSN: ISSN 0006-2960 PubMed: 15170324 DOI: 10.1021/BI049723B |
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