Zinc in PDB 1zap: Secreted Aspartic Protease From C. Albicans

All present enzymatic activity of Secreted Aspartic Protease From C. Albicans:
3.4.23.24;

The structure of Secreted Aspartic Protease From C. Albicans, PDB code: 1zap was solved by C.Abad-Zapatero, S.W.Muchmore, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.600, 98.260, 49.280, 90.00, 90.00, 90.00
R / Rfree (%)	14.5 / n/a

The binding sites of Zinc atom in the Secreted Aspartic Protease From C. Albicans (pdb code 1zap). 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 Secreted Aspartic Protease From C. Albicans, PDB code: 1zap:

Zinc binding site 1 out of 1 in the Secreted Aspartic Protease From C. Albicans


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Secreted Aspartic Protease From C. Albicans within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:17.3 occ:1.00 OD2 A:ASP57 1.8 14.6 1.0 H1 A:HOH672 2.6 12.0 1.0 CG A:ASP57 2.7 11.7 1.0 O A:HOH672 2.7 10.6 1.0 H2 A:HOH672 2.7 12.0 1.0 OD1 A:ASP57 2.9 19.1 1.0 H2 A:HOH807 3.2 12.0 1.0 O A:HOH680 3.4 10.5 1.0 H2 A:HOH680 3.9 12.0 1.0 O A:HOH807 3.9 25.8 1.0 CB A:ASP57 4.1 5.8 1.0 H1 A:HOH680 4.2 12.0 1.0 HE21 A:GLN61 4.4 12.0 1.0 OG1 A:THR55 4.5 9.6 1.0 H1 A:HOH807 4.7 12.0 1.0 NE2 A:GLN61 4.7 7.5 1.0 H A:ASP57 4.7 12.0 1.0 CB A:THR55 4.8 3.3 1.0 CD A:GLN61 5.0 8.1 1.0

C.Abad-Zapatero, R.Goldman, S.W.Muchmore, C.Hutchins, K.Stewart, J.Navaza, C.D.Payne, T.L.Ray. Structure of A Secreted Aspartic Protease From C. Albicans Complexed with A Potent Inhibitor: Implications For the Design of Antifungal Agents. Protein Sci. V. 5 640 1996.
ISSN: ISSN 0961-8368
PubMed: 8845753