Zinc in PDB 5ah0: Structure of Lipase 1 From Pelosinus Fermentans

The structure of Structure of Lipase 1 From Pelosinus Fermentans, PDB code: 5ah0 was solved by A.Hromic, K.Gruber, A.Biundo, D.Ribitsch, F.Quartinello, V.Perz, M.S.Arrell, F.Kalman, G.M.Guebitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.20 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.800, 91.800, 215.900, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 24.3

The structure of Structure of Lipase 1 From Pelosinus Fermentans also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Zinc atom in the Structure of Lipase 1 From Pelosinus Fermentans (pdb code 5ah0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Lipase 1 From Pelosinus Fermentans, PDB code: 5ah0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Lipase 1 From Pelosinus Fermentans


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Lipase 1 From Pelosinus Fermentans within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1401 b:83.4 occ:1.00 OD1 A:ASP71 1.9 76.2 1.0 OD2 A:ASP248 2.0 72.5 1.0 NE2 A:HIS97 2.1 80.1 1.0 NE2 A:HIS91 2.1 83.1 1.0 CG A:ASP71 2.8 74.3 1.0 CG A:ASP248 2.8 74.5 1.0 OD1 A:ASP248 2.9 73.2 1.0 OD2 A:ASP71 3.0 76.7 1.0 CE1 A:HIS97 3.0 81.9 1.0 CD2 A:HIS91 3.0 75.8 1.0 CD2 A:HIS97 3.1 79.5 1.0 CE1 A:HIS91 3.1 79.5 1.0 ND1 A:HIS97 4.1 84.4 1.0 CB A:ASP71 4.1 67.8 1.0 CG A:HIS91 4.2 84.7 1.0 CG A:HIS97 4.2 84.5 1.0 ND1 A:HIS91 4.2 75.4 1.0 CB A:ASP248 4.2 75.4 1.0 CD1 A:TRP70 4.4 70.9 1.0 N A:ASP71 4.6 60.6 1.0 O A:ASP248 4.7 68.2 1.0 CA A:ASP71 4.7 64.8 1.0 CG A:LYS95 4.7 81.8 1.0 CB A:LYS95 4.8 82.3 1.0 CB A:SER68 4.8 71.6 1.0

Zinc binding site 2 out of 2 in the Structure of Lipase 1 From Pelosinus Fermentans


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Lipase 1 From Pelosinus Fermentans within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1403 b:82.5 occ:1.00 OD1 B:ASP71 1.9 72.8 1.0 OD2 B:ASP248 2.0 73.8 1.0 NE2 B:HIS97 2.1 93.5 1.0 NE2 B:HIS91 2.1 79.3 1.0 CG B:ASP71 2.7 77.1 1.0 CE1 B:HIS97 2.8 95.0 1.0 OD2 B:ASP71 2.9 77.5 1.0 CD2 B:HIS91 2.9 82.3 1.0 CG B:ASP248 3.0 73.1 1.0 CD2 B:HIS97 3.2 80.1 1.0 CE1 B:HIS91 3.2 79.7 1.0 OD1 B:ASP248 3.3 72.9 1.0 ND1 B:HIS97 3.9 79.1 1.0 CG B:HIS91 4.1 84.6 1.0 CG B:HIS97 4.1 81.3 1.0 CB B:ASP71 4.2 74.8 1.0 ND1 B:HIS91 4.2 82.9 1.0 CD1 B:TRP70 4.2 80.1 1.0 CB B:ASP248 4.3 72.6 1.0 CG B:LYS95 4.7 84.8 1.0 CB B:LYS95 4.7 87.2 1.0 CA B:ASP71 4.8 69.4 1.0 N B:ASP71 4.8 69.5 1.0 O B:ASP248 4.8 80.2 1.0 CB B:SER68 4.9 72.2 1.0 CZ2 B:TRP220 4.9 71.8 1.0 NE1 B:TRP70 5.0 81.2 1.0

A.Biundo, A.Hromic, T.Pavkov-Keller, K.Gruber, F.Quartinello, K.Haernvall, V.Perz, M.S.Arrell, M.Zinn, D.Ribitsch, G.M.Guebitz. Characterization of A Poly(Butylene Adipate-Co-Terephthalate)-Hydrolyzing Lipase From Pelosinus Fermentans. Appl.Microbiol.Biotechnol. V. 100 1753 2016.
ISSN: ISSN 0175-7598
PubMed: 26490551
DOI: 10.1007/S00253-015-7031-1