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Zinc in PDB 2iej: Human Protein Farnesyltransferase Complexed with Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution

Enzymatic activity of Human Protein Farnesyltransferase Complexed with Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution

All present enzymatic activity of Human Protein Farnesyltransferase Complexed with Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution:
2.5.1.58; 2.5.1.59;

Protein crystallography data

The structure of Human Protein Farnesyltransferase Complexed with Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution, PDB code: 2iej 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) 33.69 / 1.80
Space group P 61
Cell size a, b, c (Å), α, β, γ (°) 178.253, 178.253, 64.661, 90.00, 90.00, 120.00
R / Rfree (%) 16.3 / 18.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Protein Farnesyltransferase Complexed with Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution (pdb code 2iej). 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 Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution, PDB code: 2iej:

Zinc binding site 1 out of 1 in 2iej

Go back to Zinc Binding Sites List in 2iej
Zinc binding site 1 out of 1 in the Human Protein Farnesyltransferase Complexed with Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution


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 Inhibitor Compound Stn-48 and Fpp Analog at 1.8A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn939

b:17.7
occ:1.00
 OD1 B:ASP797 2.0 14.6 1.0
NE2 B:HIS862 2.0 14.5 1.0
NAW B:S48943 2.2 19.2 1.0
SG B:CYS799 2.4 16.3 1.0
OD2 B:ASP797 2.4 14.1 1.0
CG B:ASP797 2.5 13.4 1.0
CD2 B:HIS862 3.0 15.1 1.0
CE1 B:HIS862 3.1 15.4 1.0
CAO B:S48943 3.1 23.8 1.0
CAN B:S48943 3.2 22.0 1.0
CB B:CYS799 3.3 15.3 1.0
CE2 B:TYR861 3.9 13.7 1.0
CB B:ASP797 4.0 14.3 1.0
N B:CYS799 4.0 14.8 1.0
CG B:HIS862 4.1 14.7 1.0
ND1 B:HIS862 4.1 13.4 1.0
NBK B:S48943 4.2 25.3 1.0
CA B:CYS799 4.3 14.6 1.0
CBD B:S48943 4.3 21.5 1.0
CB B:ASP852 4.3 16.5 1.0
CG B:ASP852 4.5 17.6 1.0
O B:HOH1228 4.5 18.9 1.0
OH B:TYR861 4.5 15.6 1.0
OD2 B:ASP852 4.6 21.0 1.0
O B:HOH1169 4.6 54.7 1.0
CZ B:TYR861 4.7 16.0 1.0
CH3 B:ACT940 4.8 27.3 1.0
CD2 B:TYR861 4.8 12.8 1.0
CA B:ASP852 4.8 16.9 1.0
OD1 B:ASP852 5.0 19.9 1.0

Reference:

R.T.Eastman, J.White, O.Hucke, K.Yokoyama, C.L.Verlinde, M.A.Hast, L.S.Beese, M.H.Gelb, P.K.Rathod, W.C.Van Voorhis. Resistance Mutations at the Lipid Substrate Binding Site of Plasmodium Falciparum Protein Farnesyltransferase. Mol.Biochem.Parasitol. V. 152 66 2007.
ISSN: ISSN 0166-6851
PubMed: 17208314
DOI: 10.1016/J.MOLBIOPARA.2006.11.012
Page generated: Wed Dec 16 03:31:10 2020

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