Zinc in PDB 4ar1: Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution.

The structure of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution., PDB code: 4ar1 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)	46.33 / 2.01
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.050, 108.230, 51.270, 90.00, 90.00, 90.00
R / Rfree (%)	20.028 / 24.953

The structure of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution. also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Zinc atom in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution. (pdb code 4ar1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution., PDB code: 4ar1:

Zinc binding site 1 out of 1 in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum at 2.01 Angstrom Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1722 b:26.1 occ:1.00 OE1 A:GLU487 2.0 24.2 1.0 OD2 A:ASP421 2.0 34.5 1.0 NE2 A:HIS455 2.0 25.7 1.0 NE2 A:HIS459 2.0 26.8 1.0 CG A:ASP421 2.5 34.1 1.0 CD A:GLU487 2.8 23.0 1.0 OD1 A:ASP421 2.9 38.8 1.0 CE1 A:HIS455 3.0 23.9 1.0 CD2 A:HIS459 3.0 25.9 1.0 OE2 A:GLU487 3.0 26.4 1.0 CD2 A:HIS455 3.0 24.4 1.0 CE1 A:HIS459 3.0 26.0 1.0 CB A:ASP421 3.6 31.1 1.0 ND1 A:HIS455 4.1 21.5 1.0 O A:HOH2053 4.1 30.4 1.0 CG A:HIS459 4.1 24.7 1.0 CG A:HIS455 4.1 23.1 1.0 ND1 A:HIS459 4.1 25.1 1.0 CE2 A:TYR538 4.3 26.8 1.0 CB A:ALA490 4.3 18.3 1.0 CG A:GLU487 4.3 25.6 1.0 O A:HOH2056 4.3 31.7 1.0 OH A:TYR538 4.3 26.7 1.0 OE2 A:GLU456 4.3 27.4 1.0 ND2 A:ASN424 4.6 30.6 1.0 CZ A:TYR538 4.6 27.5 1.0 CA A:GLU487 4.7 22.6 1.0 CB A:GLU487 4.7 24.8 1.0 CA A:ASP421 4.9 31.4 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