Zinc in PDB 2zog: Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin

All present enzymatic activity of Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin:
3.4.13.18;

The structure of Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin, PDB code: 2zog was solved by H.Unno, T.Yamashita, N.Okumura, M.Kusunoki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.34 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.417, 199.779, 55.495, 90.00, 118.52, 90.00
R / Rfree (%)	19.7 / 24

The binding sites of Zinc atom in the Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin (pdb code 2zog). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin, PDB code: 2zog:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin


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 Mouse Carnosinase CN2 Complexed with Zn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2001 b:25.1 occ:1.00 OD1 A:ASP132 2.1 22.1 1.0 NE2 A:HIS445 2.1 21.4 1.0 O2 A:BES1080 2.2 21.2 1.0 OE2 A:GLU167 2.2 23.9 1.0 O3 A:BES1080 2.4 22.0 1.0 OE1 A:GLU167 2.4 20.9 1.0 CD A:GLU167 2.6 24.1 1.0 C3 A:BES1080 2.9 25.7 1.0 C2 A:BES1080 3.0 22.6 1.0 CG A:ASP132 3.0 20.2 1.0 CE1 A:HIS445 3.1 22.7 1.0 CD2 A:HIS445 3.2 22.6 1.0 OD2 A:ASP132 3.3 19.2 1.0 C1 A:BES1080 3.5 24.3 1.0 ZN A:ZN2002 3.6 25.4 1.0 N2 A:BES1080 4.0 26.1 1.0 O A:HOH2014 4.0 21.5 1.0 OE1 A:GLU166 4.1 29.6 1.0 N1 A:BES1080 4.1 22.1 1.0 CG A:GLU167 4.1 24.5 1.0 ND1 A:HIS445 4.2 23.5 1.0 CG A:HIS445 4.3 22.6 1.0 CB A:ASP132 4.5 20.9 1.0 CG A:GLN103 4.5 25.3 1.0 CE1 A:HIS99 4.5 24.0 1.0 NE2 B:HIS228 4.5 24.3 1.0 NE2 A:HIS99 4.6 19.6 1.0 C4 A:BES1080 4.8 24.6 1.0 OE1 A:GLN103 4.8 28.0 1.0 CD2 B:HIS228 4.8 23.1 1.0 C6 A:BES1080 4.9 25.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin


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 Mouse Carnosinase CN2 Complexed with Zn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2002 b:25.4 occ:1.00 O2 A:BES1080 2.1 21.2 1.0 OD2 A:ASP132 2.1 19.2 1.0 NE2 A:HIS99 2.1 19.6 1.0 OD1 A:ASP195 2.3 22.2 1.0 N2 A:BES1080 2.4 26.1 1.0 OD2 A:ASP195 2.4 21.0 1.0 CG A:ASP195 2.7 19.6 1.0 C2 A:BES1080 2.9 22.6 1.0 CE1 A:HIS99 3.1 24.0 1.0 C1 A:BES1080 3.1 24.3 1.0 CG A:ASP132 3.1 20.2 1.0 CD2 A:HIS99 3.2 20.7 1.0 OD1 A:ASP132 3.6 22.1 1.0 ZN A:ZN2001 3.6 25.1 1.0 OE1 A:GLU166 3.6 29.6 1.0 OE2 A:GLU167 4.1 23.9 1.0 O A:HOH2004 4.1 22.0 1.0 CB A:ASP133 4.2 20.0 1.0 ND1 A:HIS99 4.2 19.4 1.0 CD A:GLU166 4.2 28.8 1.0 CB A:ASP195 4.2 17.0 1.0 C3 A:BES1080 4.2 25.7 1.0 CG A:HIS99 4.3 21.5 1.0 O A:ASP195 4.3 21.4 1.0 C6 A:BES1080 4.4 25.3 1.0 CB A:ASP132 4.4 20.9 1.0 OE2 A:GLU166 4.5 27.1 1.0 CA A:ASP132 4.6 20.0 1.0 OH A:TYR197 4.6 26.4 1.0 CG A:ASP133 4.6 20.7 1.0 O3 A:BES1080 4.7 22.0 1.0 CD A:GLU167 4.8 24.1 1.0 C A:ASP132 4.8 19.1 1.0 CA A:ASP195 4.9 18.9 1.0 C A:ASP195 5.0 20.9 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn3001 b:22.8 occ:1.00 OD1 B:ASP132 2.0 19.5 1.0 NE2 B:HIS445 2.2 21.1 1.0 OE2 B:GLU167 2.2 20.8 1.0 O2 B:BES1081 2.3 24.3 1.0 O3 B:BES1081 2.3 20.2 1.0 OE1 B:GLU167 2.5 20.8 1.0 CD B:GLU167 2.7 22.8 1.0 C3 B:BES1081 2.9 24.7 1.0 C2 B:BES1081 3.0 24.1 1.0 CG B:ASP132 3.0 18.7 1.0 CE1 B:HIS445 3.2 21.1 1.0 CD2 B:HIS445 3.2 21.4 1.0 OD2 B:ASP132 3.4 17.5 1.0 C1 B:BES1081 3.5 24.3 1.0 ZN B:ZN3002 3.6 22.6 1.0 N2 B:BES1081 4.0 19.6 1.0 N1 B:BES1081 4.1 21.9 1.0 CG B:GLU167 4.1 20.2 1.0 OE1 B:GLU166 4.1 24.3 1.0 O B:HOH3014 4.2 18.4 1.0 ND1 B:HIS445 4.3 22.9 1.0 CG B:HIS445 4.3 20.9 1.0 CB B:ASP132 4.4 19.4 1.0 CE1 B:HIS99 4.5 17.1 1.0 CG B:GLN103 4.6 21.2 1.0 NE2 B:HIS99 4.6 14.7 1.0 NE2 A:HIS228 4.7 22.7 1.0 OE1 B:GLN103 4.8 27.4 1.0 C4 B:BES1081 4.8 27.3 1.0 CD2 A:HIS228 4.8 22.2 1.0 C6 B:BES1081 4.8 24.5 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Mouse Carnosinase CN2 Complexed with Zn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn3002 b:22.6 occ:1.00 O2 B:BES1081 2.1 24.3 1.0 OD2 B:ASP132 2.1 17.5 1.0 OD1 B:ASP195 2.2 20.6 1.0 NE2 B:HIS99 2.2 14.7 1.0 OD2 B:ASP195 2.4 18.8 1.0 N2 B:BES1081 2.4 19.6 1.0 CG B:ASP195 2.7 16.5 1.0 C2 B:BES1081 2.9 24.1 1.0 CE1 B:HIS99 3.1 17.1 1.0 CG B:ASP132 3.1 18.7 1.0 C1 B:BES1081 3.1 24.3 1.0 CD2 B:HIS99 3.2 18.9 1.0 OD1 B:ASP132 3.5 19.5 1.0 ZN B:ZN3001 3.6 22.8 1.0 OE1 B:GLU166 3.7 24.3 1.0 CB B:ASP133 4.1 18.3 1.0 OE2 B:GLU167 4.1 20.8 1.0 CB B:ASP195 4.2 16.9 1.0 ND1 B:HIS99 4.3 17.6 1.0 C3 B:BES1081 4.3 24.7 1.0 CD B:GLU166 4.3 26.8 1.0 O B:HOH3007 4.3 22.3 1.0 CB B:ASP132 4.3 19.4 1.0 CG B:HIS99 4.3 17.6 1.0 C6 B:BES1081 4.4 24.5 1.0 O B:ASP195 4.4 17.3 1.0 CA B:ASP132 4.5 18.6 1.0 OE2 B:GLU166 4.6 27.5 1.0 OH B:TYR197 4.6 23.8 1.0 CG B:ASP133 4.7 15.9 1.0 O3 B:BES1081 4.7 20.2 1.0 C B:ASP132 4.8 18.2 1.0 CD B:GLU167 4.8 22.8 1.0 CA B:ASP195 4.9 16.7 1.0 C B:ASP195 5.0 18.8 1.0

H.Unno, T.Yamashita, S.Ujita, N.Okumura, H.Otani, A.Okumura, K.Nagai, M.Kusunoki. Structural Basis For Substrate Recognition and Hydrolysis By Mouse Carnosinase CN2. J.Biol.Chem. V. 283 27289 2008.
ISSN: ISSN 0021-9258
PubMed: 18550540
DOI: 10.1074/JBC.M801657200