Manganese in PDB 2zof: Crystal Structure of Mouse Carnosinase CN2 Complexed with Mn and Bestatin

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

The structure of Crystal Structure of Mouse Carnosinase CN2 Complexed with Mn and Bestatin, PDB code: 2zof 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)	43.03 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	54.496, 199.181, 55.215, 90.00, 118.92, 90.00
R / Rfree (%)	19.2 / 23.9

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

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Mouse Carnosinase CN2 Complexed with Mn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2001 b:30.5 occ:1.00 OD1 A:ASP132 2.1 27.8 1.0 NE2 A:HIS445 2.2 30.3 1.0 O2 A:BES1080 2.2 32.6 1.0 OE1 A:GLU167 2.3 33.1 1.0 OE2 A:GLU167 2.3 33.3 1.0 O3 A:BES1080 2.4 26.4 1.0 CD A:GLU167 2.6 34.1 1.0 CG A:ASP132 2.9 29.3 1.0 C3 A:BES1080 3.0 30.3 1.0 CE1 A:HIS445 3.1 28.9 1.0 OD2 A:ASP132 3.1 31.2 1.0 C2 A:BES1080 3.1 28.8 1.0 CD2 A:HIS445 3.2 31.1 1.0 MN A:MN2002 3.7 33.1 1.0 C1 A:BES1080 3.7 27.8 1.0 O A:HOH2184 4.0 27.6 1.0 CG A:GLU167 4.1 32.3 1.0 N2 A:BES1080 4.2 26.1 1.0 N1 A:BES1080 4.2 35.4 1.0 OE1 A:GLU166 4.2 37.7 1.0 ND1 A:HIS445 4.3 30.4 1.0 CG A:HIS445 4.3 31.8 1.0 CB A:ASP132 4.3 29.1 1.0 CG A:GLN103 4.4 35.1 1.0 CE1 A:HIS99 4.5 30.1 1.0 NE2 A:HIS99 4.6 28.2 1.0 NE2 B:HIS228 4.7 29.6 1.0 OE1 A:GLN103 4.7 41.6 1.0 C4 A:BES1080 4.9 34.6 1.0 O A:HOH2185 4.9 28.3 1.0 CD2 B:HIS228 4.9 29.7 1.0 CB A:GLU167 5.0 33.6 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Mouse Carnosinase CN2 Complexed with Mn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn2002 b:33.1 occ:1.00 OD2 A:ASP132 2.0 31.2 1.0 OD1 A:ASP195 2.1 32.3 1.0 O2 A:BES1080 2.2 32.6 1.0 NE2 A:HIS99 2.2 28.2 1.0 OD2 A:ASP195 2.4 34.2 1.0 N2 A:BES1080 2.5 26.1 1.0 CG A:ASP195 2.6 31.8 1.0 C2 A:BES1080 3.1 28.8 1.0 CG A:ASP132 3.1 29.3 1.0 CE1 A:HIS99 3.2 30.1 1.0 CD2 A:HIS99 3.2 30.0 1.0 C1 A:BES1080 3.4 27.8 1.0 OD1 A:ASP132 3.7 27.8 1.0 MN A:MN2001 3.7 30.5 1.0 OE1 A:GLU166 3.9 37.7 1.0 CB A:ASP133 4.0 29.1 1.0 O A:HOH2014 4.1 28.6 1.0 CB A:ASP195 4.1 29.9 1.0 OE2 A:GLU167 4.2 33.3 1.0 ND1 A:HIS99 4.3 28.3 1.0 CB A:ASP132 4.3 29.1 1.0 O A:ASP195 4.3 30.5 1.0 CG A:HIS99 4.3 30.9 1.0 C3 A:BES1080 4.4 30.3 1.0 CD A:GLU166 4.4 35.2 1.0 CA A:ASP132 4.5 29.1 1.0 CG A:ASP133 4.5 30.5 1.0 C6 A:BES1080 4.6 26.8 1.0 OH A:TYR197 4.6 34.8 1.0 OE2 A:GLU166 4.7 36.6 1.0 C A:ASP132 4.7 29.2 1.0 O3 A:BES1080 4.7 26.4 1.0 CA A:ASP195 4.8 30.8 1.0 CD A:GLU167 4.9 34.1 1.0 CA A:ASP133 4.9 29.8 1.0 OD2 A:ASP133 4.9 28.9 1.0 C A:ASP195 4.9 31.2 1.0 OD1 A:ASP133 4.9 33.2 1.0 N A:ASP133 5.0 28.8 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Mouse Carnosinase CN2 Complexed with Mn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn3001 b:31.8 occ:1.00 OD1 B:ASP132 2.1 27.8 1.0 NE2 B:HIS445 2.2 30.3 1.0 O2 B:BES1081 2.2 26.9 1.0 O3 B:BES1081 2.3 33.0 1.0 OE1 B:GLU167 2.3 33.1 1.0 OE2 B:GLU167 2.5 33.2 1.0 CD B:GLU167 2.7 34.1 1.0 C3 B:BES1081 2.8 33.0 1.0 C2 B:BES1081 2.9 30.5 1.0 CG B:ASP132 3.0 29.2 1.0 CE1 B:HIS445 3.1 28.9 1.0 OD2 B:ASP132 3.1 31.4 1.0 CD2 B:HIS445 3.2 31.0 1.0 C1 B:BES1081 3.7 28.9 1.0 MN B:MN3002 3.7 32.2 1.0 N1 B:BES1081 3.9 33.6 1.0 O B:HOH3162 4.1 23.4 1.0 N2 B:BES1081 4.2 24.8 1.0 OE1 B:GLU166 4.2 37.7 1.0 CG B:GLU167 4.2 32.2 1.0 ND1 B:HIS445 4.3 30.5 1.0 CG B:HIS445 4.4 31.8 1.0 CB B:ASP132 4.4 29.1 1.0 NE2 A:HIS228 4.5 29.5 1.0 CG B:GLN103 4.5 35.2 1.0 CE1 B:HIS99 4.5 30.0 1.0 NE2 B:HIS99 4.6 28.2 1.0 C4 B:BES1081 4.6 35.0 1.0 OE1 B:GLN103 4.8 41.6 1.0 CD2 A:HIS228 4.8 29.7 1.0

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


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Mouse Carnosinase CN2 Complexed with Mn and Bestatin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn3002 b:32.2 occ:1.00 O2 B:BES1081 2.0 26.9 1.0 OD1 B:ASP195 2.1 32.3 1.0 OD2 B:ASP132 2.2 31.4 1.0 NE2 B:HIS99 2.3 28.2 1.0 OD2 B:ASP195 2.3 34.2 1.0 N2 B:BES1081 2.4 24.8 1.0 CG B:ASP195 2.6 31.7 1.0 C2 B:BES1081 2.9 30.5 1.0 C1 B:BES1081 3.2 28.9 1.0 CG B:ASP132 3.2 29.2 1.0 CD2 B:HIS99 3.2 30.1 1.0 CE1 B:HIS99 3.3 30.0 1.0 MN B:MN3001 3.7 31.8 1.0 OD1 B:ASP132 3.7 27.8 1.0 OE1 B:GLU166 3.8 37.7 1.0 CB B:ASP195 4.1 29.9 1.0 CB B:ASP133 4.1 29.0 1.0 O B:HOH3163 4.2 28.2 1.0 C3 B:BES1081 4.2 33.0 1.0 OE2 B:GLU167 4.3 33.2 1.0 O B:ASP195 4.3 30.4 1.0 CD B:GLU166 4.3 35.2 1.0 ND1 B:HIS99 4.4 28.4 1.0 C6 B:BES1081 4.4 31.7 1.0 CG B:HIS99 4.4 30.9 1.0 CB B:ASP132 4.4 29.1 1.0 OE2 B:GLU166 4.5 36.6 1.0 CG B:ASP133 4.6 30.6 1.0 CA B:ASP132 4.6 29.1 1.0 OH B:TYR197 4.6 34.8 1.0 O3 B:BES1081 4.7 33.0 1.0 C B:ASP132 4.8 29.2 1.0 CA B:ASP195 4.8 30.8 1.0 CD B:GLU167 4.9 34.1 1.0 C B:ASP195 4.9 31.2 1.0 OD2 B:ASP133 4.9 28.9 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