Zinc in PDB 7t09: Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D

Enzymatic activity of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D

All present enzymatic activity of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D:
2.5.1.58;

Protein crystallography data

The structure of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D, PDB code: 7t09 was solved by Y.Wang, Y.Shi, L.S.Beese, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.82 / 1.98
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 141.915, 141.915, 130.226, 90, 90, 90
R / Rfree (%) 17.2 / 19.4

Other elements in 7t09:

The structure of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D (pdb code 7t09). 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 Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D, PDB code: 7t09:

Zinc binding site 1 out of 1 in 7t09

Go back to Zinc Binding Sites List in 7t09
Zinc binding site 1 out of 1 in the Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryptococcus Neoformans Protein Farnesyltransferase in Complex with Fpp and Inhibitor 2D within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:27.9
occ:1.00
 NE2 B:HIS410 2.1 25.3 1.0
N15 B:XMV605 2.1 27.8 1.0
OD1 B:ASP323 2.2 29.9 1.0
SG B:CYS325 2.3 24.5 1.0
OD2 B:ASP323 2.5 27.2 1.0
CG B:ASP323 2.6 27.6 1.0
CD2 B:HIS410 2.9 26.1 1.0
C16 B:XMV605 2.9 25.7 1.0
CE1 B:HIS410 3.2 27.9 1.0
C14 B:XMV605 3.2 28.1 1.0
CB B:CYS325 3.4 22.5 1.0
CE2 B:TYR409 3.9 23.8 1.0
CB B:ASP323 4.1 24.8 1.0
CG B:HIS410 4.1 27.8 1.0
N17 B:XMV605 4.1 28.3 1.0
N B:CYS325 4.2 25.2 1.0
ND1 B:HIS410 4.2 24.9 1.0
O B:HOH769 4.3 27.2 1.0
C13 B:XMV605 4.3 30.2 1.0
CB B:ASP400 4.3 28.7 1.0
O B:HOH755 4.4 43.1 1.0
CA B:CYS325 4.4 27.1 1.0
OH B:TYR409 4.4 26.0 1.0
CG B:ASP400 4.5 31.5 1.0
CZ B:TYR409 4.7 27.0 1.0
CA B:ASP400 4.7 28.4 1.0
CD2 B:TYR409 4.8 26.0 1.0
OD2 B:ASP400 4.8 32.8 1.0
OD1 B:ASP400 4.8 34.4 1.0
CE2 B:TYR326 4.9 24.4 1.0

Reference:

Y.Wang, F.Xu, C.B.Nichols, Y.Shi, H.W.Hellinga, J.A.Alspaugh, M.D.Distefano, L.S.Beese. Structure-Guided Discovery of Potent Antifungals That Prevent Ras Signaling By Inhibiting Protein Farnesyltransferase. J.Med.Chem. V. 65 13753 2022.
ISSN: ISSN 0022-2623
PubMed: 36218371
DOI: 10.1021/ACS.JMEDCHEM.2C00902
Page generated: Wed Oct 30 11:23:38 2024

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