Calcium in PDB 5o7e: Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor

The structure of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor, PDB code: 5o7e was solved by E.Schoenauer, H.Brandstetter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.33 / 1.87
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.304, 79.677, 56.959, 90.00, 91.23, 90.00
R / Rfree (%)	19 / 22.6

The structure of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Calcium atom in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor (pdb code 5o7e). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor, PDB code: 5o7e:

Calcium binding site 1 out of 1 in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor


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 H From Clostridium Histolyticum in Complex with N-Aryl Mercaptoacetamide- Based Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca802 b:16.3 occ:1.00 O A:VAL467 2.3 18.9 1.0 O A:GLY463 2.3 15.6 1.0 O A:GLY469 2.3 16.7 1.0 OE2 A:GLU430 2.4 14.9 1.0 O A:HOH924 2.4 18.3 1.0 O A:HOH930 2.4 16.8 1.0 C A:GLY463 3.3 17.2 1.0 CD A:GLU430 3.4 20.9 1.0 C A:VAL467 3.5 17.9 1.0 C A:GLY469 3.5 17.9 1.0 CA A:GLY463 3.6 13.0 1.0 OE1 A:GLU430 3.7 18.7 1.0 O A:HOH938 3.9 22.8 1.0 C A:PRO468 3.9 20.2 1.0 N A:GLY469 4.0 19.5 1.0 CA A:PRO468 4.2 17.6 1.0 N A:PRO468 4.3 18.5 1.0 O A:PRO468 4.3 17.7 1.0 CA A:GLY469 4.4 17.7 1.0 N A:GLN470 4.5 15.9 1.0 N A:ARG464 4.5 15.0 1.0 CA A:GLN470 4.6 16.9 1.0 CA A:VAL467 4.6 17.0 1.0 CB A:VAL467 4.7 15.5 1.0 OE1 A:GLU392 4.7 21.7 1.0 NE2 A:GLN470 4.7 28.1 1.0 O A:HOH967 4.7 14.8 1.0 CG A:GLU430 4.7 19.7 1.0 O A:GLN462 4.8 14.4 1.0 N A:VAL467 4.9 17.6 1.0 N A:GLY463 5.0 14.4 1.0

E.Schonauer, A.M.Kany, J.Haupenthal, K.Husecken, I.J.Hoppe, K.Voos, S.Yahiaoui, B.Elsasser, C.Ducho, H.Brandstetter, R.W.Hartmann. Discovery of A Potent Inhibitor Class with High Selectivity Toward Clostridial Collagenases. J. Am. Chem. Soc. V. 139 12696 2017.
ISSN: ESSN 1520-5126
PubMed: 28820255
DOI: 10.1021/JACS.7B06935