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Zinc in PDB 1sa5: Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662

Enzymatic activity of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662

All present enzymatic activity of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662, PDB code: 1sa5 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) 49.21 / 2.60
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 170.469, 170.469, 69.028, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 22.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662 (pdb code 1sa5). 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 Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662, PDB code: 1sa5:

Zinc binding site 1 out of 1 in 1sa5

Go back to Zinc Binding Sites List in 1sa5
Zinc binding site 1 out of 1 in the Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rat Protein Farnesyltransferase Complexed with Fpp and Bms- 214662 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn438

b:22.9
occ:1.00
NAV B:BMV440 2.1 25.5 1.0
OD2 B:ASP297 2.2 17.9 1.0
NE2 B:HIS362 2.3 23.6 1.0
SG B:CYS299 2.4 23.0 1.0
OD1 B:ASP297 2.4 14.6 1.0
CG B:ASP297 2.5 17.6 1.0
CAO B:BMV440 2.8 25.9 1.0
CD2 B:HIS362 3.1 21.4 1.0
CAP B:BMV440 3.2 26.4 1.0
CE1 B:HIS362 3.2 22.5 1.0
CB B:CYS299 3.4 21.6 1.0
CE2 B:TYR361 3.8 21.2 1.0
CB B:ASP297 4.0 16.5 1.0
NAW B:BMV440 4.0 24.9 1.0
N B:CYS299 4.1 20.8 1.0
CBA B:BMV440 4.2 24.4 1.0
CG B:HIS362 4.3 22.1 1.0
ND1 B:HIS362 4.3 23.0 1.0
CA B:CYS299 4.3 21.3 1.0
O B:HOH549 4.5 22.4 1.0
OD2 B:ASP352 4.5 29.7 1.0
CG B:ASP352 4.5 26.9 1.0
CD2 B:TYR361 4.6 21.2 1.0
CB B:ASP352 4.6 23.9 1.0
OH B:TYR361 4.7 20.6 1.0
CZ B:TYR361 4.8 20.2 1.0
CA B:ASP352 4.8 23.8 1.0
O B:HOH505 4.9 41.6 1.0
C B:ASP297 4.9 19.8 1.0
CA B:ASP297 5.0 17.5 1.0
OD1 B:ASP352 5.0 26.3 1.0

Reference:

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
Page generated: Wed Dec 16 03:03:31 2020

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