Zinc in PDB 3lq0: Zymogen Structure of Crayfish Astacin Metallopeptidase

All present enzymatic activity of Zymogen Structure of Crayfish Astacin Metallopeptidase:
3.4.24.21;

The structure of Zymogen Structure of Crayfish Astacin Metallopeptidase, PDB code: 3lq0 was solved by T.Guevara, I.Yiallouros, R.Kappelhoff, S.Bissdorf, W.Stocker, F.X.Gomis-Ruth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.92 / 1.45
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.910, 63.370, 69.190, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 18

The binding sites of Zinc atom in the Zymogen Structure of Crayfish Astacin Metallopeptidase (pdb code 3lq0). 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 Zymogen Structure of Crayfish Astacin Metallopeptidase, PDB code: 3lq0:

Zinc binding site 1 out of 1 in the Zymogen Structure of Crayfish Astacin Metallopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zymogen Structure of Crayfish Astacin Metallopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn999 b:11.8 occ:1.00 OD2 A:ASP21P 2.0 14.5 1.0 NE2 A:HIS102 2.1 13.0 1.0 NE2 A:HIS96 2.1 9.7 1.0 NE2 A:HIS92 2.1 10.3 1.0 OD1 A:ASP21P 2.3 14.4 1.0 CG A:ASP21P 2.5 11.9 1.0 CE1 A:HIS102 3.0 14.0 1.0 OH A:TYR149 3.0 20.1 1.0 CE1 A:HIS96 3.0 11.5 1.0 CD2 A:HIS92 3.0 9.3 1.0 CD2 A:HIS102 3.1 12.6 1.0 CE1 A:HIS92 3.1 9.0 1.0 CD2 A:HIS96 3.2 10.0 1.0 CZ A:TYR149 3.9 16.5 1.0 O A:HOH632 4.0 14.4 1.0 CB A:ASP21P 4.0 11.7 1.0 CE1 A:TYR149 4.1 16.2 1.0 ND1 A:HIS102 4.1 13.9 1.0 ND1 A:HIS96 4.2 11.5 1.0 CG A:HIS92 4.2 9.0 1.0 ND1 A:HIS92 4.2 7.9 1.0 CG A:HIS102 4.2 12.0 1.0 CG A:HIS96 4.3 8.5 1.0 O A:HOH634 4.7 21.7 1.0 CE A:MET147 4.7 11.2 1.0 CD2 A:LEU11P 4.9 14.3 1.0 CG1 A:ILE22P 5.0 11.9 1.0

T.Guevara, I.Yiallouros, R.Kappelhoff, S.Bissdorf, W.Stocker, F.X.Gomis-Ruth. Proenzyme Structure and Activation of Astacin Metallopeptidase J.Biol.Chem. V. 285 13958 2010.
ISSN: ISSN 0021-9258
PubMed: 20202938
DOI: 10.1074/JBC.M109.097436