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Zinc in PDB 4are: Crystal Structure of the Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution.

Enzymatic activity of Crystal Structure of the Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution.

All present enzymatic activity of Crystal Structure of the Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution.:
3.4.24.3;

Protein crystallography data

The structure of Crystal Structure of the Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution., PDB code: 4are 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) 69.50 / 2.19
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.290, 108.660, 181.000, 90.00, 90.00, 90.00
R / Rfree (%) 19.321 / 24.297

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution. (pdb code 4are). 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 Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution., PDB code: 4are:

Zinc binding site 1 out of 1 in 4are

Go back to Zinc Binding Sites List in 4are
Zinc binding site 1 out of 1 in the Crystal Structure of the Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 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 Collagenase Unit of Collagenase G From Clostridium Histolyticum at 2.19 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1790

b:52.7
occ:1.00
 OE1 A:GLU555 2.0 57.1 1.0
O A:HOH2168 2.1 40.7 1.0
NE2 A:HIS523 2.1 53.8 1.0
NE2 A:HIS527 2.1 43.1 1.0
CD2 A:HIS523 2.9 49.2 1.0
CD A:GLU555 3.0 58.9 1.0
CD2 A:HIS527 3.0 42.4 1.0
O A:HOH2169 3.1 44.7 1.0
CE1 A:HIS527 3.1 42.0 1.0
CE1 A:HIS523 3.2 56.4 1.0
OE2 A:GLU555 3.3 64.9 1.0
OE2 A:GLU524 3.5 51.1 1.0
CD A:GLU524 4.2 47.9 1.0
CG A:HIS523 4.2 46.0 1.0
CG A:HIS527 4.2 40.6 1.0
ND1 A:HIS527 4.3 42.6 1.0
ND1 A:HIS523 4.3 53.7 1.0
CG A:GLU555 4.3 55.5 1.0
CB A:ALA558 4.3 43.7 1.0
OE1 A:GLU524 4.4 51.6 1.0
CA A:GLU555 4.8 47.4 1.0
O A:HOH2152 5.0 53.2 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: Wed Dec 16 05:03:39 2020

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