Calcium in PDB 1v97: Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form

All present enzymatic activity of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form:
1.1.1.204;

The structure of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form, PDB code: 1v97 was solved by K.Okamoto, K.Matsumoto, R.Hille, B.T.Eger, E.F.Pai, T.Nishino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.94
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	167.987, 124.612, 146.926, 90.00, 90.99, 90.00
R / Rfree (%)	17.8 / 20.8

The structure of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	8 atoms

The binding sites of Calcium atom in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form (pdb code 1v97). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form, PDB code: 1v97:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca3008 b:12.0 occ:1.00 OG A:SER874 2.6 14.1 1.0 OG A:SER907 2.7 13.2 1.0 O A:ALA867 2.7 16.4 1.0 O A:SER870 2.7 12.7 1.0 O A:ASN908 2.7 13.4 1.0 O A:ARG871 2.9 13.7 1.0 C A:ARG871 3.5 12.8 1.0 N A:ASN908 3.6 14.1 1.0 C A:ALA867 3.7 14.8 1.0 C A:SER870 3.7 13.2 1.0 CB A:ASP872 3.8 14.6 1.0 C A:ASN908 3.8 13.7 1.0 CB A:SER874 3.9 12.7 1.0 CB A:SER907 3.9 11.4 1.0 C A:SER907 4.0 13.2 1.0 CB A:ALA867 4.0 14.9 1.0 CA A:SER907 4.1 12.3 1.0 NE2 A:HIS840 4.1 12.1 1.0 CA A:ALA867 4.1 14.0 1.0 CA A:ARG871 4.2 12.9 1.0 CA A:ASN908 4.2 14.2 1.0 N A:ASP872 4.2 13.9 1.0 N A:ARG871 4.4 11.9 1.0 N A:SER874 4.5 13.0 1.0 OG A:SER870 4.5 13.3 1.0 CA A:ASP872 4.5 13.2 1.0 CE1 A:HIS840 4.6 12.1 1.0 CA A:SER874 4.7 15.1 1.0 N A:SER870 4.8 14.6 1.0 O A:SER907 4.8 12.1 1.0 N A:GLY868 4.8 13.6 1.0 CB A:ASN908 4.8 12.1 1.0 CA A:SER870 4.8 14.0 1.0 N A:LEU873 4.9 13.3 1.0 CG A:ASP872 4.9 13.5 1.0 OD1 A:ASP872 5.0 13.1 1.0 N A:THR909 5.0 11.9 1.0 C A:ASP872 5.0 16.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Bovine Milk Xanthine Dehydrogenase Fyx-051 Bound Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca4008 b:16.0 occ:1.00 O B:SER870 2.6 15.9 1.0 O B:ALA867 2.6 14.2 1.0 OG B:SER874 2.6 14.4 1.0 OG B:SER907 2.7 16.5 1.0 O B:ASN908 2.7 12.0 1.0 O B:ARG871 3.0 13.4 1.0 N B:ASN908 3.5 15.1 1.0 C B:ARG871 3.5 13.5 1.0 C B:ALA867 3.7 15.4 1.0 C B:SER870 3.7 15.0 1.0 CB B:ASP872 3.7 13.8 1.0 C B:ASN908 3.8 13.7 1.0 CB B:SER907 3.9 13.2 1.0 CB B:SER874 3.9 14.2 1.0 C B:SER907 4.0 15.4 1.0 CB B:ALA867 4.0 14.1 1.0 CA B:SER907 4.1 15.3 1.0 NE2 B:HIS840 4.1 12.2 1.0 CA B:ARG871 4.1 14.2 1.0 CA B:ALA867 4.1 14.6 1.0 CA B:ASN908 4.2 14.0 1.0 N B:ASP872 4.2 14.1 1.0 N B:ARG871 4.3 13.4 1.0 OG B:SER870 4.4 14.2 1.0 N B:SER874 4.5 12.3 1.0 CA B:ASP872 4.5 14.2 1.0 CE1 B:HIS840 4.5 11.3 1.0 N B:SER870 4.7 14.3 1.0 CA B:SER874 4.8 13.6 1.0 CB B:ASN908 4.8 14.1 1.0 CA B:SER870 4.8 14.1 1.0 N B:GLY868 4.8 14.4 1.0 CG B:ASP872 4.8 17.9 1.0 O B:SER907 4.9 14.6 1.0 N B:LEU873 4.9 12.9 1.0 OD1 B:ASP872 4.9 14.1 1.0 N B:THR909 4.9 12.7 1.0 C B:ASP872 5.0 13.2 1.0

K.Okamoto, K.Matsumoto, R.Hille, B.T.Eger, E.F.Pai, T.Nishino. The Crystal Structure of Xanthine Oxidoreductase During Catalysis: Implications For Reaction Mechanism and Enzyme Inhibition. Proc.Natl.Acad.Sci.Usa V. 101 7931 2004.
ISSN: ISSN 0027-8424
PubMed: 15148401
DOI: 10.1073/PNAS.0400973101