Zinc in PDB 1sa4: Human Protein Farnesyltransferase Complexed with Fpp and R115777

All present enzymatic activity of Human Protein Farnesyltransferase Complexed with Fpp and R115777:
2.5.1.58; 2.5.1.59;

The structure of Human Protein Farnesyltransferase Complexed with Fpp and R115777, PDB code: 1sa4 was solved by T.S.Reid, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.88 / 2.10
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	178.442, 178.442, 64.458, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 19.5

The structure of Human Protein Farnesyltransferase Complexed with Fpp and R115777 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Protein Farnesyltransferase Complexed with Fpp and R115777 (pdb code 1sa4). 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 Human Protein Farnesyltransferase Complexed with Fpp and R115777, PDB code: 1sa4:

Zinc binding site 1 out of 1 in the Human Protein Farnesyltransferase Complexed with Fpp and R115777


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Protein Farnesyltransferase Complexed with Fpp and R115777 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn439 b:18.7 occ:1.00 OD2 B:ASP297 2.0 18.7 1.0 NE2 B:HIS362 2.1 17.9 1.0 N2 B:JAN441 2.1 18.7 1.0 SG B:CYS299 2.3 16.2 1.0 OD1 B:ASP297 2.5 17.4 1.0 CG B:ASP297 2.6 19.2 1.0 CD2 B:HIS362 3.0 15.9 1.0 C2 B:JAN441 3.1 17.4 1.0 C3 B:JAN441 3.1 16.8 1.0 CE1 B:HIS362 3.1 16.5 1.0 CB B:CYS299 3.3 16.0 1.0 CE2 B:TYR361 3.8 18.0 1.0 CB B:ASP297 4.0 18.4 1.0 O B:HOH676 4.1 42.9 1.0 N B:CYS299 4.1 17.4 1.0 CG B:HIS362 4.1 16.5 1.0 C4 B:JAN441 4.2 19.4 1.0 ND1 B:HIS362 4.2 15.4 1.0 N1 B:JAN441 4.2 19.3 1.0 CA B:CYS299 4.3 16.3 1.0 OH B:TYR361 4.4 19.4 1.0 O B:HOH516 4.5 16.1 1.0 CG B:ASP352 4.5 21.0 1.0 OD2 B:ASP352 4.6 24.0 1.0 CB B:ASP352 4.6 20.8 1.0 CZ B:TYR361 4.6 19.2 1.0 CD2 B:TYR361 4.7 16.9 1.0 CA B:ASP352 4.8 20.4 1.0

T.S.Reid, L.S.Beese. Crystal Structures of the Anticancer Clinical Candidates R115777 (Tipifarnib) and Bms-214662 Complexed with Protein Farnesyltransferase Suggest A Mechanism of Fti Selectivity. Biochemistry V. 43 6877 2004.
ISSN: ISSN 0006-2960
PubMed: 15170324
DOI: 10.1021/BI049723B