Zinc in PDB 4arf: Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution.

Enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution.

All present enzymatic activity of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution.:
3.4.24.3;

Protein crystallography data

The structure of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution., PDB code: 4arf 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) 40.00 / 1.77
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.870, 106.780, 51.350, 90.00, 90.00, 90.00
R / Rfree (%) 15 / 20

Other elements in 4arf:

The structure of Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution. also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution. (pdb code 4arf). 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 in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution., PDB code: 4arf:

Zinc binding site 1 out of 1 in 4arf

Go back to Zinc Binding Sites List in 4arf
Zinc binding site 1 out of 1 in the Crystal Structure of the Peptidase Domain of Collagenase H From Clostridium Histolyticum in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 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 in Complex with the Peptidic Inhibitor Isoamylphosphonyl-Gly-Pro-Ala at 1.77 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn801

b:20.8
occ:1.00
 O2 B:IP81 2.0 22.9 1.0
OE1 A:GLU487 2.0 21.2 1.0
NE2 A:HIS459 2.0 22.0 1.0
NE2 A:HIS455 2.1 20.2 1.0
CD A:GLU487 2.8 21.6 1.0
OE2 A:GLU487 2.9 21.1 1.0
O B:IP81 3.0 23.4 1.0
P1 B:IP81 3.0 21.6 1.0
CE1 A:HIS459 3.0 19.1 1.0
CD2 A:HIS459 3.0 20.5 1.0
CD2 A:HIS455 3.0 19.6 1.0
CE1 A:HIS455 3.1 19.4 1.0
OH A:TYR538 4.0 20.9 1.0
CE2 A:TYR538 4.0 20.4 1.0
N B:GLY2 4.0 22.3 1.0
CA B:GLY2 4.1 22.2 1.0
ND1 A:HIS459 4.1 19.4 1.0
CG A:HIS459 4.2 18.3 1.0
ND1 A:HIS455 4.2 18.8 1.0
CG A:GLU487 4.2 20.2 1.0
CG A:HIS455 4.2 19.1 1.0
O1 B:IP81 4.2 29.8 1.0
CZ A:TYR538 4.4 22.1 1.0
CB A:ALA490 4.4 17.9 1.0
OE2 A:GLU456 4.6 21.7 1.0
CA A:GLU487 4.7 17.5 1.0
O B:HOH101 4.7 21.8 1.0
CB A:GLU487 4.7 17.7 1.0
CD2 A:TYR538 5.0 20.6 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 19:22:25 2024

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