Zinc in PDB 1o1t: Structure of Fpt Bound to the Cvim-Fpp Product

The structure of Structure of Fpt Bound to the Cvim-Fpp Product, PDB code: 1o1t was solved by T.C.Turek-Etienne, C.L.Strickland, M.D.Distefano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	171.440, 171.440, 69.220, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / n/a

The structure of Structure of Fpt Bound to the Cvim-Fpp Product also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Structure of Fpt Bound to the Cvim-Fpp Product (pdb code 1o1t). 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 Structure of Fpt Bound to the Cvim-Fpp Product, PDB code: 1o1t:

Zinc binding site 1 out of 1 in the Structure of Fpt Bound to the Cvim-Fpp Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Fpt Bound to the Cvim-Fpp Product within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2001 b:28.6 occ:1.00 OD2 B:ASP297 2.0 19.3 1.0 NE2 B:HIS362 2.3 18.8 1.0 SG B:CYS299 2.3 23.1 1.0 OD1 B:ASP297 2.5 21.5 1.0 CG B:ASP297 2.6 17.7 1.0 SG B:2NH3001 2.7 53.8 1.0 CD2 B:HIS362 3.0 17.7 1.0 CB B:CYS299 3.2 20.6 1.0 CE1 B:HIS362 3.3 21.1 1.0 CB2 B:2NH3001 3.7 61.1 1.0 C B:2NH3001 3.8 51.8 1.0 CE2 B:TYR361 3.8 13.4 1.0 C2 B:2NH3001 3.9 44.3 1.0 N B:CYS299 4.0 22.7 1.0 CB B:ASP297 4.0 15.8 1.0 CA B:CYS299 4.2 19.9 1.0 CG B:HIS362 4.2 19.9 1.0 ND1 B:HIS362 4.3 22.6 1.0 O B:HOH3110 4.4 51.1 1.0 OH B:TYR361 4.5 21.8 1.0 CB B:ASP352 4.6 26.1 1.0 CG B:ASP352 4.6 22.9 1.0 CD2 B:TYR361 4.7 12.4 1.0 OD2 B:ASP352 4.7 29.6 1.0 CZ B:TYR361 4.7 16.5 1.0 O B:HOH3095 4.8 44.4 1.0 CA B:ASP352 4.8 23.4 1.0 C1 B:2NH3001 4.9 43.4 1.0

T.C.Turek-Etienne, C.L.Strickland, M.D.Distefano. Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights Into Isoprenoid Recognition By Protein Farnesyl Transferase Biochemistry V. 42 3716 2003.
ISSN: ISSN 0006-2960
PubMed: 12667062
DOI: 10.1021/BI0266838