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Zinc in PDB 4lnb: Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5

Enzymatic activity of Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5

All present enzymatic activity of Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5:
2.5.1.58;

Protein crystallography data

The structure of Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5, PDB code: 4lnb was solved by M.F.Mabanglo, 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) 37.07 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.321, 91.253, 83.052, 90.00, 110.93, 90.00
R / Rfree (%) 15.9 / 18.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5 (pdb code 4lnb). 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 Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5, PDB code: 4lnb:

Zinc binding site 1 out of 1 in 4lnb

Go back to Zinc Binding Sites List in 4lnb
Zinc binding site 1 out of 1 in the Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and 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 Aspergillus Fumigatus Protein Farnesyltransferase Ternary Complex with Farnesyldiphosphate and Ethylenediamine Scaffold Inhibitor 5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn602

b:11.8
occ:1.00
 OD2 B:ASP387 2.0 15.0 1.0
NE2 B:HIS455 2.0 9.9 1.0
NBC B:ED5603 2.1 11.1 1.0
SG B:CYS389 2.4 10.7 1.0
OD1 B:ASP387 2.5 8.3 1.0
CG B:ASP387 2.6 10.0 1.0
CD2 B:HIS455 2.9 11.2 1.0
CAT B:ED5603 2.9 9.8 1.0
CAS B:ED5603 3.1 13.4 1.0
CE1 B:HIS455 3.1 13.0 1.0
CB B:CYS389 3.3 11.8 1.0
CE2 B:TYR454 3.8 11.0 1.0
CB B:ASP387 4.0 8.9 1.0
CG B:HIS455 4.1 10.4 1.0
NBO B:ED5603 4.1 13.5 1.0
ND1 B:HIS455 4.1 10.8 1.0
CBI B:ED5603 4.2 14.3 1.0
N B:CYS389 4.2 8.3 1.0
CA B:CYS389 4.4 8.2 1.0
CG B:ASP445 4.4 18.3 1.0
OH B:TYR454 4.5 13.7 1.0
O B:HOH704 4.5 9.9 1.0
CB B:ASP445 4.6 16.5 1.0
OD2 B:ASP445 4.6 18.9 1.0
CD2 B:TYR454 4.6 9.0 1.0
CZ B:TYR454 4.6 11.1 1.0
OD1 B:ASP445 4.8 14.7 1.0
CA B:ASP445 4.8 14.6 1.0

Reference:

M.F.Mabanglo, M.A.Hast, N.B.Lubock, H.W.Hellinga, L.S.Beese. Crystal Structures of the Fungal Pathogen Aspergillus Fumigatus Protein Farnesyltransferase Complexed with Substrates and Inhibitors Reveal Features For Antifungal Drug Design. Protein Sci. V. 23 289 2014.
ISSN: ISSN 0961-8368
PubMed: 24347326
DOI: 10.1002/PRO.2411
Page generated: Sun Oct 27 02:02:46 2024

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