Zinc in PDB 7v6f: Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P

All present enzymatic activity of Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P:
4.1.2.13;

The structure of Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P, PDB code: 7v6f was solved by C.Hongxuan, Y.Huang, C.Han, W.Chen, Y.Ren, J.Wan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.68 / 2.98
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	119.458, 56.57, 131.747, 90, 113.43, 90
R / Rfree (%)	21.7 / 28

The binding sites of Zinc atom in the Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P (pdb code 7v6f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P, PDB code: 7v6f:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:59.6 occ:1.00 NE2 A:HIS109 2.1 28.5 1.0 OE1 A:GLU173 2.2 56.5 1.0 OE2 A:GLU173 2.2 51.2 1.0 NE2 A:HIS225 2.3 77.9 1.0 ND1 A:HIS264 2.4 45.9 1.0 CD A:GLU173 2.4 50.6 1.0 CE1 A:HIS225 2.7 73.6 1.0 CE1 A:HIS109 3.0 29.2 1.0 CD2 A:HIS109 3.1 29.0 1.0 CE1 A:HIS264 3.2 45.3 1.0 CD2 A:HIS225 3.5 81.5 1.0 CG A:HIS264 3.5 44.4 1.0 CB A:HIS264 3.9 42.0 1.0 ND1 A:HIS225 3.9 83.1 1.0 CG A:GLU173 3.9 46.5 1.0 ND1 A:HIS109 4.1 28.6 1.0 CG A:HIS109 4.2 27.4 1.0 O A:HOH708 4.2 12.6 1.0 CG A:HIS225 4.3 86.2 1.0 NE2 A:HIS264 4.4 47.0 1.0 CD2 A:HIS264 4.6 47.5 1.0 OD1 A:ASP143 4.7 41.6 1.0 CB A:GLU173 4.7 45.5 1.0 CE A:MET141 5.0 43.1 1.0 CG A:ASP143 5.0 44.7 1.0

Zinc binding site 2 out of 2 in the Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Complexed with G3P within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:68.5 occ:1.00 NE2 B:HIS109 1.8 55.6 1.0 NE2 B:HIS225 2.1 65.8 1.0 OE2 B:GLU173 2.2 48.2 1.0 OE1 B:GLU173 2.2 52.1 1.0 ND1 B:HIS264 2.4 45.3 1.0 CD B:GLU173 2.5 50.8 1.0 CE1 B:HIS109 2.8 55.0 1.0 CD2 B:HIS109 2.8 53.2 1.0 CD2 B:HIS225 2.9 71.5 1.0 CE1 B:HIS225 2.9 66.1 1.0 CE1 B:HIS264 3.2 47.4 1.0 CG B:HIS264 3.5 43.5 1.0 ND1 B:HIS225 3.8 64.4 1.0 CG B:HIS225 3.8 72.0 1.0 ND1 B:HIS109 3.9 55.1 1.0 CG B:GLU173 3.9 51.5 1.0 CG B:HIS109 3.9 52.0 1.0 CB B:HIS264 3.9 44.3 1.0 OD1 B:ASP143 4.3 49.5 1.0 CE B:MET141 4.4 44.7 1.0 CB B:GLU173 4.4 54.4 1.0 NE2 B:HIS264 4.4 47.2 1.0 OD2 B:ASP143 4.4 49.4 1.0 CG B:ASP143 4.5 52.7 1.0 CD2 B:HIS264 4.6 44.2 1.0

W.Wen, H.Cao, Y.Huang, J.Tu, C.Wan, J.Wan, X.Han, H.Chen, J.Liu, L.Rao, C.Su, C.Peng, C.Sheng, Y.Ren. Structure-Guided Discovery of the Novel Covalent Allosteric Site and Covalent Inhibitors of Fructose-1,6-Bisphosphate Aldolase to Overcome the Azole Resistance of Candidiasis. J.Med.Chem. V. 65 2656 2022.
ISSN: ISSN 0022-2623
DOI: 10.1021/ACS.JMEDCHEM.1C02102