Zinc in PDB 1ft1: Crystal Structure of Protein Farnesyltransferase at 2.25 Angstroms Resolution

The structure of Crystal Structure of Protein Farnesyltransferase at 2.25 Angstroms Resolution, PDB code: 1ft1 was solved by L.S.Beese, H.-W.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.25
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	167.060, 167.060, 97.900, 90.00, 90.00, 120.00
R / Rfree (%)	21 / 26

The binding sites of Zinc atom in the Crystal Structure of Protein Farnesyltransferase at 2.25 Angstroms Resolution (pdb code 1ft1). 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 Crystal Structure of Protein Farnesyltransferase at 2.25 Angstroms Resolution, PDB code: 1ft1:

Zinc binding site 1 out of 1 in the Crystal Structure of Protein Farnesyltransferase at 2.25 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Protein Farnesyltransferase at 2.25 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:27.5 occ:1.00 OD2 B:ASP297 2.0 21.2 1.0 SG B:CYS299 2.2 19.2 1.0 NE2 B:HIS362 2.5 20.1 1.0 OD1 B:ASP297 2.6 26.0 1.0 CG B:ASP297 2.6 23.5 1.0 O B:HOH1002 2.7 21.3 1.0 CD2 B:HIS362 3.2 18.6 1.0 CE1 B:HIS362 3.5 21.1 1.0 CB B:CYS299 3.5 18.4 1.0 CE2 B:TYR361 4.0 18.1 1.0 CB B:ASP297 4.1 21.0 1.0 N B:CYS299 4.2 19.3 1.0 CG B:HIS362 4.4 19.7 1.0 CA B:CYS299 4.5 18.9 1.0 ND1 B:HIS362 4.5 21.4 1.0 O B:HOH1341 4.6 34.8 1.0 CG B:ASP352 4.6 20.7 1.0 OH B:TYR361 4.6 19.7 1.0 CB B:ASP352 4.6 21.2 1.0 OD2 B:ASP352 4.8 22.4 1.0 CD2 B:TYR361 4.8 17.5 1.0 CZ B:TYR361 4.8 18.1 1.0 CA B:ASP352 4.8 23.0 1.0 OD1 B:ASP352 4.9 22.6 1.0 CE2 B:TYR300 5.0 24.5 1.0

H.W.Park, S.R.Boduluri, J.F.Moomaw, P.J.Casey, L.S.Beese. Crystal Structure of Protein Farnesyltransferase at 2.25 Angstrom Resolution. Science V. 275 1800 1997.
ISSN: ISSN 0036-8075
PubMed: 9065406
DOI: 10.1126/SCIENCE.275.5307.1800