Zinc in PDB 3dra: Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp

All present enzymatic activity of Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp:
2.5.1.58; 2.5.1.59;

The structure of Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp, PDB code: 3dra 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)	37.64 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	132.304, 66.049, 82.821, 90.00, 100.02, 90.00
R / Rfree (%)	19.2 / 23.1

The binding sites of Zinc atom in the Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp (pdb code 3dra). 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 Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp, PDB code: 3dra:

Zinc binding site 1 out of 1 in the Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Candida Albicans Protein Geranylgeranyltransferase-I Complexed with Ggpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn391 b:27.4 occ:1.00 CE1 B:HIS349 2.1 16.6 1.0 OD2 B:ASP294 2.2 18.2 1.0 OD1 B:ASP294 2.4 18.8 1.0 SG B:CYS296 2.5 23.6 1.0 CG B:ASP294 2.6 15.6 1.0 O B:HOH5342 2.7 35.9 1.0 ND1 B:HIS349 3.1 20.7 1.0 NE2 B:HIS349 3.1 21.4 1.0 CB B:CYS296 3.4 17.9 1.0 NE B:ARG339 4.1 35.4 1.0 CG B:ARG339 4.1 24.1 1.0 CB B:ASP294 4.1 15.7 1.0 N B:CYS296 4.1 15.8 1.0 O B:HOH3198 4.3 33.8 1.0 CG B:HIS349 4.3 17.5 1.0 CD B:ARG339 4.3 30.5 1.0 CD2 B:HIS349 4.3 18.8 1.0 CA B:CYS296 4.4 17.3 1.0 CE B:MET348 4.4 27.5 1.0 O B:HOH5090 4.6 26.4 1.0 CZ B:ARG339 4.8 38.6 1.0 CB B:ARG339 4.9 20.9 1.0

M.A.Hast, L.S.Beese. Structure of Protein Geranylgeranyltransferase-I From the Human Pathogen Candida Albicans Complexed with A Lipid Substrate. J.Biol.Chem. V. 283 31933 2008.
ISSN: ISSN 0021-9258
PubMed: 18713740
DOI: 10.1074/JBC.M805330200