Zinc in PDB 4on1: Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis

The structure of Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis, PDB code: 4on1 was solved by A.E.Aleshin, R.C.Liddington, S.A.Shiryaev, A.Y.Strongin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.32 / 2.13
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.424, 114.395, 140.213, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 20

The binding sites of Zinc atom in the Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis (pdb code 4on1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis, PDB code: 4on1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis


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 Metalloproteinase-II From Bacteroides Fragilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:19.9 occ:1.00 NE2 A:HIS361 2.0 21.7 1.0 NE2 A:HIS355 2.0 14.0 1.0 NE2 A:HIS351 2.0 13.7 1.0 OD2 A:ASP193 2.2 28.9 1.0 OD1 A:ASP193 2.3 21.3 1.0 CG A:ASP193 2.5 18.9 1.0 CD2 A:HIS351 2.9 13.8 1.0 CD2 A:HIS361 3.0 17.0 1.0 CE1 A:HIS361 3.0 17.9 1.0 CD2 A:HIS355 3.0 14.3 1.0 CE1 A:HIS355 3.0 23.6 1.0 CE1 A:HIS351 3.1 21.6 1.0 CG2 A:ILE191 3.6 48.3 1.0 ND1 A:HIS361 4.0 26.9 1.0 CB A:ASP193 4.1 18.4 1.0 CG A:HIS361 4.1 23.1 1.0 CG A:HIS351 4.1 15.4 1.0 ND1 A:HIS355 4.1 14.4 1.0 CG A:HIS355 4.1 14.0 1.0 ND1 A:HIS351 4.1 16.3 1.0 CD2 A:TYR194 4.5 24.7 1.0 CB A:ILE191 4.5 61.0 1.0 O A:HOH651 4.5 41.3 1.0 O A:HOH573 4.5 34.9 1.0 CE2 A:TYR194 4.5 26.2 1.0 CE A:MET369 4.6 17.6 1.0 N A:ASP193 4.9 35.3 1.0 CA A:ASP193 4.9 19.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Metalloproteinase-II From Bacteroides Fragilis within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn400 b:18.8 occ:1.00 NE2 B:HIS361 2.0 20.4 1.0 NE2 B:HIS351 2.0 15.6 1.0 NE2 B:HIS355 2.0 13.8 1.0 OD1 B:ASP193 2.2 23.4 1.0 OD2 B:ASP193 2.2 26.2 1.0 CG B:ASP193 2.5 21.5 1.0 CD2 B:HIS351 2.9 12.5 1.0 CE1 B:HIS361 2.9 19.2 1.0 CD2 B:HIS355 2.9 12.8 1.0 CD2 B:HIS361 3.0 15.3 1.0 CE1 B:HIS355 3.0 20.5 1.0 CE1 B:HIS351 3.1 17.9 1.0 CG2 B:ILE191 3.4 48.0 1.0 ND1 B:HIS361 4.0 24.9 1.0 CB B:ASP193 4.1 21.6 1.0 CG B:HIS361 4.1 20.5 1.0 CG B:HIS351 4.1 15.7 1.0 ND1 B:HIS351 4.1 18.4 1.0 CG B:HIS355 4.1 12.8 1.0 ND1 B:HIS355 4.1 15.7 1.0 CD2 B:TYR194 4.3 23.3 1.0 CE2 B:TYR194 4.3 25.9 1.0 CB B:ILE191 4.4 58.6 1.0 CE B:MET369 4.7 14.2 1.0 N B:ASP193 4.7 35.0 1.0 O B:HOH537 4.8 32.4 1.0 CA B:ASP193 4.9 22.6 1.0

S.A.Shiryaev, A.E.Aleshin, N.Muranaka, M.Kukreja, D.A.Routenberg, A.G.Remacle, R.C.Liddington, P.Cieplak, I.A.Kozlov, A.Y.Strongin. Structural and Functional Diversity of Metalloproteinases Encoded By the Bacteroides Fragilis Pathogenicity Island. Febs J. V. 281 2487 2014.
ISSN: ISSN 1742-464X
PubMed: 24698179
DOI: 10.1111/FEBS.12804