Calcium in PDB 2c1v: Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form

All present enzymatic activity of Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form:
1.11.1.5;

The structure of Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form, PDB code: 2c1v was solved by A.Echalier, V.Fulop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.22 / 1.2
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.370, 141.200, 51.580, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 18.8

The structure of Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Calcium atom in the Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form (pdb code 2c1v). 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 the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form, PDB code: 2c1v:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence 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 the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca403 b:7.9 occ:1.00 O A:PRO272 2.3 9.6 1.0 O A:HOH2191 2.3 9.3 1.0 O A:THR270 2.4 9.3 1.0 OD1 A:ASN93 2.4 9.7 1.0 O A:HOH2501 2.4 9.2 1.0 O A:HOH2500 2.4 7.9 1.0 O A:HOH2415 2.5 8.5 1.0 CG A:ASN93 3.4 9.4 1.0 C A:PRO272 3.6 9.4 1.0 C A:THR270 3.6 10.0 1.0 ND2 A:ASN93 3.8 9.5 1.0 C A:ALA271 4.2 9.4 1.0 CB A:THR270 4.2 9.2 1.0 N A:PRO272 4.3 9.0 1.0 OG1 A:THR270 4.3 10.1 1.0 CA A:TYR273 4.3 9.5 1.0 O A:ALA94 4.3 9.5 1.0 N A:TYR273 4.4 9.8 1.0 O A:HOH2192 4.4 9.5 1.0 CA A:THR270 4.5 9.8 1.0 CA A:ALA271 4.5 9.6 1.0 O A:ALA271 4.5 9.4 1.0 O2A A:HEC402 4.5 10.6 1.0 N A:ALA271 4.5 9.7 1.0 CA A:PRO272 4.6 9.0 1.0 CD1 A:TYR273 4.6 10.3 1.0 O A:HOH2193 4.6 10.3 1.0 O1A A:HEC402 4.7 10.8 1.0 CB A:ASN93 4.7 9.8 1.0 CD A:PRO272 4.8 9.5 1.0 O A:HOH2502 4.9 21.2 1.0 CE1 A:TYR273 5.0 9.1 1.0 O A:PHE274 5.0 10.1 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence 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 the Di-Haem Cytochrome C Peroxidase From Paracoccus Pantotrophus - Mixed Valence Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca403 b:10.6 occ:1.00 O B:HOH2218 2.3 10.6 1.0 O B:PRO272 2.3 13.3 1.0 O B:THR270 2.4 12.8 1.0 O B:HOH2540 2.4 11.4 1.0 OD1 B:ASN93 2.4 11.4 1.0 O B:HOH2446 2.4 10.9 1.0 O B:HOH2539 2.4 11.3 1.0 CG B:ASN93 3.4 9.3 1.0 C B:PRO272 3.6 12.4 1.0 C B:THR270 3.6 13.4 1.0 ND2 B:ASN93 3.8 11.0 1.0 C B:ALA271 4.2 13.0 1.0 CB B:THR270 4.2 12.8 1.0 N B:PRO272 4.3 12.6 1.0 O B:ALA94 4.4 10.1 1.0 OG1 B:THR270 4.4 12.9 1.0 CA B:TYR273 4.4 12.6 1.0 N B:TYR273 4.4 12.9 1.0 O B:ALA271 4.4 12.9 1.0 O B:HOH2217 4.5 12.0 1.0 CA B:ALA271 4.5 13.1 1.0 CA B:THR270 4.5 13.0 1.0 N B:ALA271 4.5 13.1 1.0 CA B:PRO272 4.5 13.3 1.0 O2A B:HEC402 4.5 12.7 1.0 O B:HOH2220 4.6 12.3 1.0 CD1 B:TYR273 4.6 12.9 1.0 O1A B:HEC402 4.7 13.2 1.0 CB B:ASN93 4.7 10.2 1.0 CD B:PRO272 4.8 13.3 1.0 O B:HOH2538 5.0 22.1 1.0 O B:PHE274 5.0 13.1 1.0 CE1 B:TYR273 5.0 13.0 1.0

A.Echalier, C.F.Goodhew, G.W.Pettigrew, V.Fulop. Activation and Catalysis of the Di-Heme Cytochrome C Peroxidase From Paracoccus Pantotrophus Structure V. 14 107 2006.
ISSN: ISSN 0969-2126
PubMed: 16407070
DOI: 10.1016/J.STR.2005.09.011