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Zinc in PDB 3e37: Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5

Enzymatic activity of Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5

All present enzymatic activity of Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5, PDB code: 3e37 was solved by M.A.Hast, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.84 / 1.80
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 178.386, 178.386, 64.510, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 19

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5 (pdb code 3e37). 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 Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5, PDB code: 3e37:

Zinc binding site 1 out of 1 in 3e37

Go back to Zinc Binding Sites List in 3e37
Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Protein Farnesyltransferase Complexed with Bisubstrate Ethylenediamine Scaffold Inhibitor 5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:14.7
occ:1.00
 NBC B:ED51 2.0 19.5 1.0
NE2 B:HIS364 2.1 12.6 1.0
OD1 B:ASP299 2.1 16.4 1.0
SG B:CYS301 2.3 12.2 1.0
OD2 B:ASP299 2.4 13.6 1.0
CG B:ASP299 2.6 13.0 1.0
CAT B:ED51 3.0 20.8 1.0
CD2 B:HIS364 3.0 13.2 1.0
CAS B:ED51 3.1 19.6 1.0
CE1 B:HIS364 3.1 13.5 1.0
CB B:CYS301 3.3 11.1 1.0
CE2 B:TYR363 3.9 11.8 1.0
N B:CYS301 4.0 10.5 1.0
CB B:ASP299 4.0 12.3 1.0
CBI B:ED51 4.1 20.9 1.0
NBO B:ED51 4.2 21.7 1.0
ND1 B:HIS364 4.2 11.3 1.0
CG B:HIS364 4.2 11.6 1.0
CA B:CYS301 4.2 10.4 1.0
CB B:ASP354 4.4 13.8 1.0
CG B:ASP354 4.5 15.9 1.0
OD2 B:ASP354 4.5 17.5 1.0
OH B:TYR363 4.5 14.2 1.0
O B:HOH7724 4.7 26.7 1.0
CZ B:TYR363 4.7 12.5 1.0
O B:HOH8037 4.8 52.8 1.0
CD2 B:TYR363 4.8 10.3 1.0
CA B:ASP354 4.8 14.3 1.0
CE1 B:TYR302 4.9 18.4 1.0
C B:ASP299 5.0 11.8 1.0
OD1 B:ASP354 5.0 15.5 1.0

Reference:

M.A.Hast, S.Fletcher, C.G.Cummings, E.E.Pusateri, M.A.Blaskovich, K.Rivas, M.H.Gelb, W.C.Van Voorhis, S.M.Sebti, A.D.Hamilton, L.S.Beese. Structural Basis For Binding and Selectivity of Antimalarial and Anticancer Ethylenediamine Inhibitors to Protein Farnesyltransferase. Chem.Biol. V. 16 181 2009.
ISSN: ISSN 1074-5521
PubMed: 19246009
DOI: 10.1016/J.CHEMBIOL.2009.01.014
Page generated: Thu Oct 24 12:35:31 2024

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