Zinc in PDB 1fpp: Protein Farnesyltransferase Complex with Farnesyl Diphosphate

The structure of Protein Farnesyltransferase Complex with Farnesyl Diphosphate, PDB code: 1fpp was solved by P.Dunten, U.Kammlott, R.Crowther, D.Weber, R.Palermo, J.Birktoft, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.75
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	170.000, 170.000, 68.860, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 30

The binding sites of Zinc atom in the Protein Farnesyltransferase Complex with Farnesyl Diphosphate (pdb code 1fpp). 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 Complex with Farnesyl Diphosphate, PDB code: 1fpp:

Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complex with Farnesyl Diphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Protein Farnesyltransferase Complex with Farnesyl Diphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn438 b:20.8 occ:1.00 OD2 B:ASP297 2.0 17.6 1.0 OD1 B:ASP297 2.0 10.0 1.0 NE2 B:HIS362 2.1 14.4 1.0 SG B:CYS299 2.3 9.2 1.0 CG B:ASP297 2.3 7.3 1.0 CE1 B:HIS362 3.0 8.6 1.0 CD2 B:HIS362 3.1 9.7 1.0 O B:HOH443 3.2 18.4 1.0 CB B:CYS299 3.4 14.6 1.0 CB B:ASP297 3.8 9.5 1.0 CE2 B:TYR361 3.9 6.9 1.0 N B:CYS299 4.0 15.5 1.0 ND1 B:HIS362 4.1 8.6 1.0 CG B:HIS362 4.2 5.3 1.0 CA B:CYS299 4.3 13.4 1.0 CG B:ASP352 4.4 24.0 1.0 CB B:ASP352 4.4 28.1 1.0 OD2 B:ASP352 4.4 27.6 1.0 OH B:TYR361 4.6 8.3 1.0 CA B:ASP352 4.7 22.7 1.0 CZ B:TYR361 4.8 8.0 1.0 C B:ASP297 4.8 18.7 1.0 CA B:ASP297 4.8 18.0 1.0 CE2 B:TYR300 4.8 20.4 1.0 CD2 B:TYR361 4.8 6.5 1.0 OD1 B:ASP352 4.9 22.0 1.0 CD2 B:TYR300 4.9 18.6 1.0 O B:ASP297 5.0 18.9 1.0

P.Dunten, U.Kammlott, R.Crowther, D.Weber, R.Palermo, J.Birktoft. Protein Farnesyltransferase: Structure and Implications For Substrate Binding. Biochemistry V. 37 7907 1998.
ISSN: ISSN 0006-2960
PubMed: 9609683
DOI: 10.1021/BI980531O