Zinc in PDB 3dpy: Protein Farnesyltransferase Complexed with Fpp and Caged Tkcvim Substrate

All present enzymatic activity of Protein Farnesyltransferase Complexed with Fpp and Caged Tkcvim Substrate:
2.5.1.58; 2.5.1.59;

The structure of Protein Farnesyltransferase Complexed with Fpp and Caged Tkcvim Substrate, PDB code: 3dpy was solved by M.A.Hast, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.20 / 2.70
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	171.491, 171.491, 69.529, 90.00, 90.00, 120.00
R / Rfree (%)	21.5 / 25.3

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with Fpp and Caged Tkcvim Substrate (pdb code 3dpy). 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 Fpp and Caged Tkcvim Substrate, PDB code: 3dpy:

Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with Fpp and Caged Tkcvim Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Protein Farnesyltransferase Complexed with Fpp and Caged Tkcvim Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:44.5 occ:1.00 OD1 B:ASP297 1.9 35.5 1.0 NE2 B:HIS362 2.3 41.0 1.0 SG B:CYS299 2.4 37.9 1.0 CG B:ASP297 2.5 37.4 1.0 OD2 B:ASP297 2.6 37.2 1.0 CE1 B:HIS362 3.1 40.9 1.0 CD2 B:HIS362 3.2 40.9 1.0 CB B:CYS299 3.4 38.1 1.0 O B:HOH3027 3.4 39.2 1.0 CE2 B:TYR361 3.7 36.9 1.0 CB B:ASP297 4.0 37.7 1.0 ND1 B:HIS362 4.2 41.1 1.0 N B:CYS299 4.2 38.0 1.0 CG B:HIS362 4.3 41.3 1.0 OH B:TYR361 4.3 35.2 1.0 CA B:CYS299 4.4 38.2 1.0 CZ B:TYR361 4.5 36.3 1.0 CD2 B:TYR361 4.6 36.7 1.0 CB B:ASP352 4.6 48.4 1.0 OD2 B:ASP352 4.6 48.8 1.0 CG B:ASP352 4.7 48.7 1.0

A.J.Degraw, M.A.Hast, J.Xu, D.Mullen, L.S.Beese, G.Barany, M.D.Distefano. Caged Protein Prenyltransferase Substrates: Tools For Understanding Protein Prenylation. Chem.Biol.Drug Des. V. 72 171 2008.
ISSN: ISSN 1747-0277
PubMed: 18844669
DOI: 10.1111/J.1747-0285.2008.00698.X