Calcium in PDB 4ar8: Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution.

The structure of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution., PDB code: 4ar8 was solved by U.Eckhard, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.75 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.420, 102.080, 102.480, 90.00, 90.00, 90.00
R / Rfree (%)	21.765 / 26.793

The structure of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution. also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution. (pdb code 4ar8). 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 Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution., PDB code: 4ar8:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution.


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 Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1732 b:25.2 occ:1.00 OE2 A:GLU440 2.3 24.7 1.0 O A:ILE477 2.3 22.9 1.0 O A:GLY473 2.3 22.5 1.0 O A:GLY479 2.3 24.8 1.0 O A:HOH2036 2.3 27.1 1.0 O A:HOH2055 2.4 22.7 1.0 C A:GLY473 3.2 21.2 1.0 CD A:GLU440 3.4 23.8 1.0 CA A:GLY473 3.5 21.5 1.0 C A:ILE477 3.5 23.4 1.0 C A:GLY479 3.6 23.2 1.0 OE1 A:GLU440 3.7 25.8 1.0 O A:HOH2038 3.9 32.8 1.0 C A:PRO478 4.0 23.7 1.0 N A:GLY479 4.1 25.6 1.0 O A:PRO478 4.4 22.6 1.0 CA A:PRO478 4.4 24.4 1.0 N A:PRO478 4.4 23.4 1.0 CA A:GLY479 4.4 26.3 1.0 N A:ARG474 4.5 23.0 1.0 CA A:ILE477 4.5 22.6 1.0 N A:LEU480 4.5 28.1 1.0 CB A:ILE477 4.5 22.6 1.0 CA A:LEU480 4.6 27.9 1.0 O A:HOH2034 4.6 32.5 1.0 CG A:GLU440 4.7 24.3 1.0 O A:GLN472 4.7 18.5 1.0 N A:GLY473 4.8 20.9 1.0 N A:ILE477 4.8 21.9 1.0 OE1 A:GLU402 4.9 34.8 1.0 CG2 A:ILE477 5.0 23.2 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution.


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 Peptidase Domain of Collagenase T From Clostridium Tetani Complexed with the Peptidic Inhibitor Isoamyl- Phosphonyl-Gly-Pro-Ala at 2.05 Angstrom Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1732 b:30.0 occ:1.00 O B:ILE477 2.3 29.9 1.0 O B:GLY473 2.3 26.1 1.0 O B:GLY479 2.3 32.3 1.0 OE2 B:GLU440 2.3 33.3 1.0 O B:HOH2045 2.3 28.7 1.0 O B:HOH2027 2.4 28.5 1.0 C B:GLY473 3.3 25.2 1.0 CD B:GLU440 3.4 33.0 1.0 C B:ILE477 3.5 29.6 1.0 C B:GLY479 3.5 29.0 1.0 CA B:GLY473 3.6 24.9 1.0 OE1 B:GLU440 3.8 33.8 1.0 C B:PRO478 4.0 33.3 1.0 N B:GLY479 4.0 35.5 1.0 O B:HOH2031 4.1 31.6 1.0 CA B:PRO478 4.3 31.5 1.0 O B:PRO478 4.3 34.3 1.0 N B:PRO478 4.4 31.1 1.0 CA B:GLY479 4.4 34.9 1.0 N B:ARG474 4.5 27.6 1.0 N B:LEU480 4.5 35.6 1.0 CA B:ILE477 4.5 26.9 1.0 CB B:ILE477 4.6 26.1 1.0 CA B:LEU480 4.6 35.5 1.0 O B:HOH2024 4.6 31.6 1.0 CG B:GLU440 4.7 32.7 1.0 O B:GLN472 4.8 23.2 1.0 N B:ILE477 4.8 28.8 1.0 N B:GLY473 4.9 25.7 1.0 OE1 B:GLU402 4.9 57.0 1.0

U.Eckhard, E.Schonauer, H.Brandstetter. Structural Basis For Activity Regulation and Substrate Preference of Clostridial Collagenases G, H, and T. J.Biol.Chem. V. 288 20184 2013.
ISSN: ISSN 0021-9258
PubMed: 23703618
DOI: 10.1074/JBC.M112.448548