Zinc in PDB 1af0: Serratia Protease in Complex with Inhibitor

All present enzymatic activity of Serratia Protease in Complex with Inhibitor:
3.4.24.40;

The structure of Serratia Protease in Complex with Inhibitor, PDB code: 1af0 was solved by U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	151.000, 109.200, 42.600, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / n/a

The structure of Serratia Protease in Complex with Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

7 atoms

The binding sites of Zinc atom in the Serratia Protease in Complex with Inhibitor (pdb code 1af0). 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 Serratia Protease in Complex with Inhibitor, PDB code: 1af0:

Zinc binding site 1 out of 1 in the Serratia Protease in Complex with Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Serratia Protease in Complex with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn472 b:19.6 occ:1.00 NE2 A:HIS186 2.1 21.5 1.0 NE2 A:HIS180 2.1 16.4 1.0 NE2 A:HIS176 2.1 17.7 1.0 O1 A:0Z9674 2.1 30.2 1.0 OH A:0Z9674 2.1 35.9 1.0 C1 A:0Z9674 2.8 31.9 1.0 N2 A:0Z9674 2.9 30.6 1.0 CD2 A:HIS186 3.0 20.4 1.0 CD2 A:HIS176 3.0 17.6 1.0 CE1 A:HIS180 3.0 15.4 1.0 CD2 A:HIS180 3.1 15.4 1.0 CE1 A:HIS186 3.1 20.9 1.0 CE1 A:HIS176 3.1 19.1 1.0 CG A:HIS186 4.1 20.3 1.0 ND1 A:HIS180 4.1 15.3 1.0 CE1 A:TYR216 4.2 31.8 1.0 ND1 A:HIS186 4.2 21.9 1.0 CG A:HIS176 4.2 17.2 1.0 ND1 A:HIS176 4.2 17.6 1.0 OH A:TYR216 4.2 37.1 1.0 CG A:HIS180 4.2 14.6 1.0 CA1 A:0Z9674 4.2 30.5 1.0 OE2 A:GLU177 4.4 22.8 1.0 N1 A:0Z9674 4.6 29.7 1.0 CZ A:TYR216 4.6 34.5 1.0 O A:0Z9674 4.6 28.8 1.0 OE1 A:GLU177 4.7 22.8 1.0 C A:0Z9674 4.7 31.5 1.0 O A:HOH2126 4.9 50.1 1.0 CE A:MET214 4.9 20.9 1.0 CD A:GLU177 5.0 18.1 1.0

U.Baumann, U.Baumann. N/A N/A.