Zinc in PDB 1ft2: Co-Crystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate

The structure of Co-Crystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate, PDB code: 1ft2 was solved by L.S.Beese, P.J.Casey, S.B.Long, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 3.40
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	166.660, 166.660, 98.820, 90.00, 90.00, 120.00
R / Rfree (%)	21.9 / 26.8

The binding sites of Zinc atom in the Co-Crystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate (pdb code 1ft2). 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 Co-Crystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate, PDB code: 1ft2:

Zinc binding site 1 out of 1 in the Co-Crystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Co-Crystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1001 b:47.8 occ:1.00 OD2 B:ASP297 2.4 21.4 1.0 SG B:CYS299 2.4 13.9 1.0 NE2 B:HIS362 2.6 35.6 1.0 CG B:ASP297 3.0 21.8 1.0 OD1 B:ASP297 3.0 18.7 1.0 CE1 B:HIS362 3.4 36.9 1.0 CE2 B:TYR361 3.4 23.0 1.0 CD2 B:HIS362 3.5 26.6 1.0 CB B:CYS299 3.7 17.6 1.0 OH B:TYR361 3.9 26.7 1.0 CZ B:TYR361 4.1 24.8 1.0 ND1 B:HIS362 4.4 31.4 1.0 CD2 B:TYR361 4.4 27.2 1.0 CB B:ASP297 4.4 22.8 1.0 CG B:HIS362 4.5 22.9 1.0 CE2 B:TYR300 4.8 29.3 1.0 N B:CYS299 4.8 20.6 1.0 CG B:ASP352 4.8 48.9 1.0 CA B:CYS299 4.9 19.2 1.0 OD2 B:ASP352 4.9 49.4 1.0

S.B.Long, P.J.Casey, L.S.Beese. Cocrystal Structure of Protein Farnesyltransferase Complexed with A Farnesyl Diphosphate Substrate. Biochemistry V. 37 9612 1998.
ISSN: ISSN 0006-2960
PubMed: 9657673
DOI: 10.1021/BI980708E