Zinc in PDB 3q73: Cryptococcus Neoformans Protein Farnesyltransferase, Apo Enzyme

The structure of Cryptococcus Neoformans Protein Farnesyltransferase, Apo Enzyme, PDB code: 3q73 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)	33.07 / 2.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	144.041, 144.041, 130.444, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22

The binding sites of Zinc atom in the Cryptococcus Neoformans Protein Farnesyltransferase, Apo Enzyme (pdb code 3q73). 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, Apo Enzyme, PDB code: 3q73:

Zinc binding site 1 out of 1 in the Cryptococcus Neoformans Protein Farnesyltransferase, Apo Enzyme


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, Apo Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn521 b:38.4 occ:1.00 NE2 B:HIS410 2.1 35.0 1.0 OD2 B:ASP323 2.2 35.9 1.0 O B:HOH2583 2.4 33.7 1.0 SG B:CYS325 2.5 33.7 1.0 OD1 B:ASP323 2.7 34.9 1.0 CG B:ASP323 2.7 34.6 1.0 CD2 B:HIS410 3.0 34.7 1.0 CE1 B:HIS410 3.1 36.4 1.0 CB B:CYS325 3.4 32.1 1.0 CE2 B:TYR409 3.9 33.7 1.0 CG B:HIS410 4.1 34.9 1.0 ND1 B:HIS410 4.1 36.0 1.0 CB B:ASP323 4.2 34.3 1.0 CB B:ASP400 4.2 35.7 1.0 O B:HOH2092 4.2 32.8 1.0 N B:CYS325 4.4 32.3 1.0 CG B:ASP400 4.5 37.0 1.0 CA B:CYS325 4.5 32.0 1.0 CD2 B:TYR409 4.7 33.9 1.0 O B:HOH2128 4.7 51.5 1.0 OH B:TYR409 4.7 34.8 1.0 CA B:ASP400 4.7 35.3 1.0 OD2 B:ASP400 4.8 38.6 1.0 CZ B:TYR409 4.8 34.1 1.0 OD1 B:ASP400 4.8 37.7 1.0

M.A.Hast, C.B.Nichols, S.M.Armstrong, S.M.Kelly, H.W.Hellinga, J.A.Alspaugh, L.S.Beese. Structures of Cryptococcus Neoformans Protein Farnesyltransferase Reveal Strategies For Developing Inhibitors That Target Fungal Pathogens. J.Biol.Chem. V. 286 35149 2011.
ISSN: ISSN 0021-9258
PubMed: 21816822
DOI: 10.1074/JBC.M111.250506