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Zinc in PDB 1s63: Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp

Enzymatic activity of Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp

All present enzymatic activity of Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp, PDB code: 1s63 was solved by S.B.Long, P.J.Casey, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.67 / 1.90
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 178.247, 178.247, 64.518, 90.00, 90.00, 120.00
R / Rfree (%) 16.1 / 18.4

Other elements in 1s63:

The structure of Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp (pdb code 1s63). 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 L-778,123 and Fpp, PDB code: 1s63:

Zinc binding site 1 out of 1 in 1s63

Go back to Zinc Binding Sites List in 1s63
Zinc binding site 1 out of 1 in the Human Protein Farnesyltransferase Complexed with L-778,123 and Fpp


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 L-778,123 and Fpp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:13.6
occ:1.00
 OD2 B:ASP297 2.0 11.1 1.0
N18 B:7783012 2.0 13.2 1.0
NE2 B:HIS362 2.1 12.2 1.0
SG B:CYS299 2.3 10.5 1.0
OD1 B:ASP297 2.5 11.9 1.0
CG B:ASP297 2.6 12.2 1.0
C17 B:7783012 3.0 12.4 1.0
CD2 B:HIS362 3.0 11.0 1.0
CE1 B:HIS362 3.1 12.4 1.0
C12 B:7783012 3.2 13.4 1.0
CB B:CYS299 3.4 10.9 1.0
CE2 B:TYR361 3.8 9.8 1.0
CB B:ASP297 4.0 11.1 1.0
N11 B:7783012 4.1 12.5 1.0
N B:CYS299 4.1 11.2 1.0
CG B:HIS362 4.1 10.9 1.0
ND1 B:HIS362 4.1 10.8 1.0
C7 B:7783012 4.2 13.7 1.0
O B:HOH1634 4.2 30.6 1.0
O B:HOH1207 4.3 11.2 1.0
CA B:CYS299 4.3 10.1 1.0
CB B:ASP352 4.4 11.2 1.0
OH B:TYR361 4.5 13.2 1.0
CG B:ASP352 4.5 12.8 1.0
CD2 B:TYR361 4.6 9.5 1.0
CZ B:TYR361 4.6 11.2 1.0
OD2 B:ASP352 4.7 14.1 1.0
CA B:ASP352 4.8 11.9 1.0
CE1 B:TYR300 5.0 8.8 1.0
OD1 B:ASP352 5.0 11.6 1.0

Reference:

T.S.Reid, S.B.Long, L.S.Beese. Crystallographic Analysis Reveals That Anticancer Clinical Candidate L-778,123 Inhibits Protein Farnesyltransferase and Geranylgeranyltransferase-I By Different Binding Modes. Biochemistry V. 43 9000 2004.
ISSN: ISSN 0006-2960
PubMed: 15248757
DOI: 10.1021/BI049280B
Page generated: Wed Oct 16 18:44:26 2024

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