Zinc in PDB 7v6g: Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Mutation C157S with CN39

All present enzymatic activity of Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Mutation C157S with CN39:
4.1.2.13;

The structure of Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Mutation C157S with CN39, PDB code: 7v6g was solved by H.Cao, Y.Huang, H.Chen, C.Wan, Y.Ren, J.Wan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.82 / 2.34
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	160.182, 56.536, 82.034, 90, 96.07, 90
R / Rfree (%)	20.4 / 25.8

The binding sites of Zinc atom in the Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Mutation C157S with CN39 (pdb code 7v6g). 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 Mutation C157S with CN39, PDB code: 7v6g:
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 Mutation C157S with CN39


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 Mutation C157S with CN39 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:60.0 occ:1.00 OE2 A:GLU173 2.0 57.6 1.0 NE2 A:HIS225 2.1 61.9 1.0 NE2 A:HIS109 2.3 49.7 1.0 ND1 A:HIS264 2.4 47.6 1.0 OE1 A:GLU173 2.4 58.2 1.0 CD A:GLU173 2.5 51.8 1.0 O A:HOH515 2.7 56.5 1.0 CE1 A:HIS225 3.0 59.9 1.0 CD2 A:HIS109 3.1 43.4 1.0 CD2 A:HIS225 3.2 56.1 1.0 CE1 A:HIS264 3.2 57.4 1.0 CE1 A:HIS109 3.3 51.3 1.0 CG A:HIS264 3.5 52.6 1.0 CB A:HIS264 3.8 52.7 1.0 CG A:GLU173 4.0 52.9 1.0 ND1 A:HIS225 4.1 63.0 1.0 CG A:HIS225 4.2 65.0 1.0 CG A:HIS109 4.3 53.8 1.0 OD2 A:ASP143 4.4 55.3 1.0 ND1 A:HIS109 4.4 55.8 1.0 NE2 A:HIS264 4.4 54.1 1.0 CD2 A:HIS264 4.5 53.7 1.0 CB A:GLU173 4.7 51.3 1.0 CG A:ASP143 4.8 46.3 1.0

Zinc binding site 2 out of 2 in the Structure of Candida Albicans Fructose-1,6-Bisphosphate Aldolase Mutation C157S with CN39


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 Mutation C157S with CN39 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:59.3 occ:1.00 NE2 B:HIS109 1.8 61.0 1.0 NE2 B:HIS225 2.0 60.2 1.0 OE1 B:GLU173 2.2 55.9 1.0 OE2 B:GLU173 2.2 56.4 1.0 ND1 B:HIS264 2.5 57.8 1.0 CD B:GLU173 2.5 55.3 1.0 CE1 B:HIS109 2.7 54.8 1.0 CD2 B:HIS109 2.9 59.8 1.0 CD2 B:HIS225 2.9 60.4 1.0 CE1 B:HIS225 3.0 58.2 1.0 O B:HOH544 3.3 56.7 1.0 CE1 B:HIS264 3.3 61.7 1.0 CG B:HIS264 3.6 58.1 1.0 ND1 B:HIS109 3.8 63.8 1.0 CB B:HIS264 3.9 56.1 1.0 CG B:HIS109 3.9 58.3 1.0 CG B:GLU173 4.0 55.4 1.0 ND1 B:HIS225 4.1 62.4 1.0 CG B:HIS225 4.1 60.5 1.0 NE2 B:HIS264 4.5 54.7 1.0 OD2 B:ASP143 4.6 56.1 1.0 CD2 B:HIS264 4.6 52.4 1.0 CB B:GLU173 4.7 55.8 1.0 CG B:ASP143 5.0 62.4 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