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Zinc in PDB 3e34: Protein Farnesyltransferase Complexed with Fpp and Ethylenediamine-Scaffold Inhibitor 10

Enzymatic activity of Protein Farnesyltransferase Complexed with Fpp and Ethylenediamine-Scaffold Inhibitor 10

All present enzymatic activity of Protein Farnesyltransferase Complexed with Fpp and Ethylenediamine-Scaffold Inhibitor 10:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Protein Farnesyltransferase Complexed with Fpp and Ethylenediamine-Scaffold Inhibitor 10, PDB code: 3e34 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) 32.16 / 2.05
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 170.169, 170.169, 69.467, 90.00, 90.00, 120.00
R / Rfree (%) 19.2 / 21.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Protein Farnesyltransferase Complexed with Fpp and Ethylenediamine-Scaffold Inhibitor 10 (pdb code 3e34). 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 Fpp and Ethylenediamine-Scaffold Inhibitor 10, PDB code: 3e34:

Zinc binding site 1 out of 1 in 3e34

Go back to Zinc Binding Sites List in 3e34
Zinc binding site 1 out of 1 in the Protein Farnesyltransferase Complexed with Fpp and Ethylenediamine-Scaffold Inhibitor 10


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 Fpp and Ethylenediamine-Scaffold Inhibitor 10 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:17.8
occ:1.00
OD2 B:ASP297 2.1 16.3 1.0
NE2 B:HIS362 2.2 17.8 1.0
NBJ B:ED11003 2.2 21.8 1.0
SG B:CYS299 2.3 16.3 1.0
OD1 B:ASP297 2.5 15.8 1.0
CG B:ASP297 2.6 16.0 1.0
CAX B:ED11003 2.9 23.6 1.0
CD2 B:HIS362 3.1 16.1 1.0
CE1 B:HIS362 3.1 16.7 1.0
CB B:CYS299 3.3 13.1 1.0
CAW B:ED11003 3.3 21.0 1.0
CE2 B:TYR361 3.8 15.8 1.0
N B:CYS299 4.0 13.5 1.0
CB B:ASP297 4.1 14.7 1.0
NBY B:ED11003 4.2 22.4 1.0
ND1 B:HIS362 4.2 17.0 1.0
CA B:CYS299 4.2 13.9 1.0
CG B:HIS362 4.2 16.7 1.0
CB B:ASP352 4.2 19.4 1.0
CBR B:ED11003 4.4 21.5 1.0
CG B:ASP352 4.4 19.6 1.0
O B:HOH2679 4.5 20.9 1.0
OD2 B:ASP352 4.5 21.5 1.0
OH B:TYR361 4.6 21.3 1.0
CD2 B:TYR361 4.6 15.7 1.0
CZ B:TYR361 4.7 16.9 1.0
CA B:ASP352 4.7 19.5 1.0
OD1 B:ASP352 4.9 18.9 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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