Zinc in PDB 1sat: Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens

The structure of Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens, PDB code: 1sat was solved by U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.75
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 (%)	18.8 / n/a

The structure of Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens also contains other interesting chemical elements:

Calcium

(Ca)

7 atoms

The binding sites of Zinc atom in the Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens (pdb code 1sat). 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 Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens, PDB code: 1sat:

Zinc binding site 1 out of 1 in the Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the 50 kDa Metallo Protease From S. Marcescens within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn472 b:10.7 occ:0.74 O A:HOH510 1.8 19.0 1.0 NE2 A:HIS186 2.0 13.3 1.0 NE2 A:HIS176 2.1 12.1 1.0 NE2 A:HIS180 2.1 13.9 1.0 OH A:TYR216 2.8 36.8 1.0 CD2 A:HIS186 2.9 19.6 1.0 CD2 A:HIS176 3.0 11.2 1.0 CE1 A:HIS186 3.0 16.0 1.0 CE1 A:HIS176 3.1 12.5 1.0 CE1 A:HIS180 3.1 12.6 1.0 CD2 A:HIS180 3.1 13.4 1.0 CZ A:TYR216 3.7 32.8 1.0 O A:HOH511 3.9 28.7 1.0 CE2 A:TYR216 4.0 31.3 1.0 CG A:HIS186 4.0 17.2 1.0 OE2 A:GLU177 4.1 13.1 1.0 ND1 A:HIS186 4.1 17.7 1.0 ND1 A:HIS176 4.2 11.7 1.0 CG A:HIS176 4.2 11.6 1.0 ND1 A:HIS180 4.2 12.7 1.0 CG A:HIS180 4.3 12.0 1.0 OE1 A:GLU177 4.5 14.3 1.0 CD A:GLU177 4.7 13.1 1.0 O A:HOH612 4.7 29.9 1.0 CE A:MET214 4.7 11.4 1.0 CE1 A:TYR216 4.7 33.4 1.0 O A:MET214 4.9 17.6 1.0

U.Baumann, U.Baumann. N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 8089845
DOI: 10.1006/JMBI.1994.1576