Zinc in PDB 2h6s: Secreted Aspartic Proteinase (Sap) 3 From Candida Albicans

All present enzymatic activity of Secreted Aspartic Proteinase (Sap) 3 From Candida Albicans:
3.4.23.24;

The structure of Secreted Aspartic Proteinase (Sap) 3 From Candida Albicans, PDB code: 2h6s was solved by E.Ruge, C.Borelli, K.Maskos, R.Huber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.350, 61.350, 171.980, 90.00, 90.00, 120.00
R / Rfree (%)	23.4 / 26

The binding sites of Zinc atom in the Secreted Aspartic Proteinase (Sap) 3 From Candida Albicans (pdb code 2h6s). 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 Proteinase (Sap) 3 From Candida Albicans, PDB code: 2h6s:

Zinc binding site 1 out of 1 in the Secreted Aspartic Proteinase (Sap) 3 From Candida 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 Proteinase (Sap) 3 From Candida Albicans within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn602 b:27.4 occ:1.00 OD2 A:ASP214 1.9 30.4 1.0 ND1 A:HIS197 2.2 14.8 1.0 CG A:ASP214 2.8 22.0 1.0 OD1 A:ASP214 3.1 24.6 1.0 CE1 A:HIS197 3.1 25.2 1.0 CG A:HIS197 3.2 22.6 1.0 CB A:HIS197 3.5 20.3 1.0 CB A:ASP214 4.2 18.6 1.0 CA A:HIS197 4.2 22.6 1.0 NE2 A:HIS197 4.2 25.6 1.0 CD2 A:HIS197 4.3 23.1 1.0 N A:ASP214 4.3 19.7 1.0 CG2 A:THR189 4.4 21.4 1.0 CA A:ASP214 4.5 19.5 1.0 C A:VAL213 4.5 21.0 1.0 O A:VAL213 4.7 17.5 1.0 CB A:THR189 4.9 27.7 1.0 O A:HOH694 5.0 35.8 1.0 CA A:VAL213 5.0 22.0 1.0

C.Borelli, E.Ruge, M.Schaller, M.Monod, H.C.Korting, R.Huber, K.Maskos. The Crystal Structure of the Secreted Aspartic Proteinase 3 From Candida Albicans and Its Complex with Pepstatin A. Proteins V. 68 738 2007.
ISSN: ISSN 0887-3585
PubMed: 17510964
DOI: 10.1002/PROT.21425