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Zinc in PDB 4ar9: Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.

Enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.

All present enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.:
3.4.24.3;

Protein crystallography data

The structure of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution., PDB code: 4ar9 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) 38.45 / 1.69
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.890, 102.110, 104.750, 90.00, 90.00, 90.00
R / Rfree (%) 17.234 / 22.105

Other elements in 4ar9:

The structure of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution. also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution. (pdb code 4ar9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution., PDB code: 4ar9:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4ar9

Go back to Zinc Binding Sites List in 4ar9
Zinc binding site 1 out of 2 in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 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 T From Clostridium Tetani at 1.69 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1731

b:33.8
occ:1.00
 OE1 A:GLU499 2.0 23.3 1.0
O A:HOH2108 2.0 37.3 1.0
NE2 A:HIS469 2.0 17.0 1.0
NE2 A:HIS465 2.0 26.3 1.0
O A:HOH2107 2.5 22.0 1.0
CE1 A:HIS465 2.9 19.8 1.0
CE1 A:HIS469 2.9 15.0 1.0
CD2 A:HIS469 3.1 12.9 1.0
CD A:GLU499 3.1 20.3 1.0
CD2 A:HIS465 3.1 22.4 1.0
OE2 A:GLU499 3.4 26.4 1.0
OE2 A:GLU466 3.7 23.7 1.0
ND1 A:HIS469 4.1 12.6 1.0
ND1 A:HIS465 4.1 25.2 1.0
CG A:HIS469 4.2 12.5 1.0
CG A:HIS465 4.3 18.4 1.0
CD A:GLU466 4.3 20.4 1.0
O A:HOH2110 4.4 38.7 1.0
CE2 A:TYR548 4.4 23.6 1.0
CG A:GLU499 4.5 20.1 1.0
OE1 A:GLU466 4.5 19.5 1.0
CB A:ALA502 4.5 11.8 1.0
CA A:GLU499 4.8 17.4 1.0
CB A:GLU499 4.9 17.5 1.0
O A:HOH2085 5.0 20.0 1.0

Zinc binding site 2 out of 2 in 4ar9

Go back to Zinc Binding Sites List in 4ar9
Zinc binding site 2 out of 2 in the Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Peptidase Domain of Collagenase T From Clostridium Tetani at 1.69 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1731

b:20.5
occ:1.00
 OE1 B:GLU499 2.0 21.4 1.0
O B:HOH2093 2.0 24.6 1.0
NE2 B:HIS469 2.0 16.7 1.0
NE2 B:HIS465 2.0 18.1 1.0
CE1 B:HIS469 3.0 18.5 1.0
CD B:GLU499 3.0 17.9 1.0
CE1 B:HIS465 3.0 16.0 1.0
CD2 B:HIS469 3.0 15.6 1.0
CD2 B:HIS465 3.1 17.9 1.0
OE2 B:GLU499 3.3 21.6 1.0
OE2 B:GLU466 3.7 22.9 1.0
ND1 B:HIS469 4.1 17.1 1.0
ND1 B:HIS465 4.1 18.5 1.0
CG B:HIS469 4.2 13.3 1.0
CG B:HIS465 4.2 16.5 1.0
CE2 B:TYR548 4.3 24.2 1.0
CG B:GLU499 4.4 17.5 1.0
CD B:GLU466 4.4 19.3 1.0
CB B:ALA502 4.5 12.0 1.0
O B:HOH2095 4.5 45.6 1.0
OE1 B:GLU466 4.5 19.9 1.0
O B:HOH2097 4.6 50.1 1.0
CA B:GLU499 4.8 16.6 1.0
CB B:GLU499 4.8 16.1 1.0
OH B:TYR548 4.9 32.0 1.0

Reference:

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
Page generated: Sat Oct 26 19:21:05 2024

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