Calcium in PDB 4jgu: Crystal Structure of Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium

The structure of Crystal Structure of Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium, PDB code: 4jgu was solved by R.Bauer, O.Matsushita, J.Sakon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.19 / 1.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.387, 38.869, 54.657, 90.00, 98.43, 90.00
R / Rfree (%)	15 / 19.1

The binding sites of Calcium atom in the Crystal Structure of Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium (pdb code 4jgu). 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 Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium, PDB code: 4jgu:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium


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 Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca901 b:8.5 occ:1.00 OD1 A:ASP804 2.3 10.7 1.0 O A:LYS775 2.4 9.5 1.0 OD1 A:ASN774 2.4 9.6 1.0 OD2 A:ASP802 2.4 9.5 1.0 OD2 A:ASP844 2.4 7.6 1.0 OD1 A:ASP802 2.4 10.3 1.0 O A:HOH1001 2.5 9.8 1.0 CG A:ASP802 2.7 9.1 1.0 CG A:ASN774 3.3 10.1 1.0 CG A:ASP844 3.4 7.7 1.0 CG A:ASP804 3.5 12.2 1.0 ND2 A:ASN774 3.6 11.7 1.0 C A:LYS775 3.6 10.0 1.0 CB A:ASP844 4.0 7.2 1.0 OD2 A:ASP804 4.0 12.9 1.0 N A:LYS775 4.1 9.7 1.0 CB A:ASP802 4.3 8.3 1.0 OD1 A:ASP844 4.3 8.9 1.0 CA A:LYS775 4.3 9.5 1.0 O A:HOH1030 4.4 16.2 1.0 C A:ASP804 4.4 8.6 1.0 N A:GLY805 4.5 7.8 1.0 N A:ASP804 4.6 9.0 1.0 OG A:SER846 4.6 10.6 1.0 N A:LEU776 4.6 10.2 1.0 CB A:ASN774 4.7 9.1 1.0 CB A:LYS775 4.7 10.7 1.0 O A:ASP804 4.7 11.2 1.0 CB A:ASP804 4.8 10.1 1.0 C A:ASN774 4.8 12.1 1.0 CA A:GLY805 4.8 8.2 1.0 CA A:ASP804 4.8 9.5 1.0 CA A:LEU776 4.8 10.6 1.0 C A:LEU776 4.9 9.7 1.0 OG A:SER845 4.9 8.3 1.0 CA A:ASN774 5.0 9.6 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium


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 Clostridium Histolyticum Colh Collagenase Collagen-Binding Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca901 b:7.2 occ:1.00 OD1 B:ASP804 2.3 10.2 1.0 OD2 B:ASP844 2.4 6.7 1.0 O B:LYS775 2.4 7.2 1.0 O B:HOH1001 2.4 7.7 1.0 OD1 B:ASN774 2.4 8.2 1.0 OD2 B:ASP802 2.5 8.6 1.0 OD1 B:ASP802 2.5 9.4 1.0 CG B:ASP802 2.8 6.7 1.0 CG B:ASN774 3.3 7.0 1.0 CG B:ASP844 3.3 6.7 1.0 CG B:ASP804 3.5 9.9 1.0 ND2 B:ASN774 3.5 9.3 1.0 C B:LYS775 3.6 7.8 1.0 CB B:ASP844 3.9 7.5 1.0 OD2 B:ASP804 3.9 11.4 1.0 N B:LYS775 4.1 7.7 1.0 OD1 B:ASP844 4.2 6.3 1.0 CB B:ASP802 4.3 7.0 1.0 CA B:LYS775 4.4 8.0 1.0 O B:HOH1012 4.4 10.8 1.0 N B:GLY805 4.5 7.2 1.0 C B:ASP804 4.5 6.5 1.0 N B:ASP804 4.6 7.6 1.0 N B:LEU776 4.6 8.6 1.0 OG B:SER846 4.6 7.7 1.0 CB B:ASP804 4.7 8.8 1.0 CB B:ASN774 4.7 8.5 1.0 CB B:LYS775 4.7 8.9 1.0 CA B:GLY805 4.8 7.5 1.0 O B:ASP804 4.8 10.5 1.0 CA B:LEU776 4.8 9.4 1.0 CA B:ASP804 4.8 8.8 1.0 OG B:SER845 4.8 7.3 1.0 C B:ASN774 4.9 8.5 1.0 C B:LEU776 5.0 7.9 1.0

R.Bauer, O.Matsushita, J.Sakon. Crystal Structure of Clostridium Histolyticum Colh Collagenase Polycystic Kidney Disease-Like Domain 2B at 1.4 Angstrom Resolution in Presence of Calcium To Be Published.