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Calcium in PDB 4aqo: Crystal Structure of the Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution.

Enzymatic activity of Crystal Structure of the Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution.

All present enzymatic activity of Crystal Structure of the Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution.:
3.4.24.3;

Protein crystallography data

The structure of Crystal Structure of the Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution., PDB code: 4aqo 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) 35.45 / 0.99
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 19.753, 70.896, 23.379, 90.00, 95.24, 90.00
R / Rfree (%) 12.386 / 14.998

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution. (pdb code 4aqo). 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 Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution., PDB code: 4aqo:

Calcium binding site 1 out of 1 in 4aqo

Go back to Calcium Binding Sites List in 4aqo
Calcium binding site 1 out of 1 in the Crystal Structure of the Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution.


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 Calcium Bound Pkd-Like Domain of Collagenase G From Clostridium Histolyticum at 0.99 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1881

b:5.8
occ:1.00
 OD1 A:ASP825 2.3 7.3 1.0
OD2 A:ASP864 2.4 5.4 1.0
O A:LYS796 2.4 5.8 1.0
OD1 A:ASP823 2.4 8.2 1.0
OD2 A:ASP823 2.4 7.5 1.0
OD1 A:ASN795 2.4 7.5 1.0
O A:HOH2019 2.4 8.5 1.0
CG A:ASP823 2.8 6.7 1.0
CG A:ASP864 3.3 4.9 1.0
CG A:ASN795 3.4 7.3 1.0
CG A:ASP825 3.4 8.1 1.0
C A:LYS796 3.6 5.5 1.0
ND2 A:ASN795 3.6 7.0 1.0
CB A:ASP864 3.8 5.0 1.0
OD2 A:ASP825 3.9 12.1 1.0
N A:LYS796 4.1 6.2 1.0
O A:HOH2018 4.2 12.2 1.0
CB A:ASP823 4.3 7.3 1.0
OD1 A:ASP864 4.3 5.0 1.0
C A:ASP825 4.4 7.1 1.0
N A:GLY826 4.4 7.1 1.0
CA A:LYS796 4.4 6.6 1.0
N A:ALA797 4.5 5.5 1.0
N A:ASP825 4.6 7.0 1.0
C A:ALA797 4.6 5.0 1.0
CA A:ALA797 4.6 5.2 1.0
CB A:ASP825 4.7 7.2 1.0
O A:ASP825 4.7 8.0 1.0
CA A:GLY826 4.7 7.4 1.0
OD1 A:ASP865 4.7 7.0 1.0
N A:PRO798 4.7 5.0 1.0
CB A:ASN795 4.7 9.2 1.0
CA A:ASP825 4.8 7.2 1.0
CD A:PRO798 4.8 5.1 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: Tue Jul 8 18:39:19 2025

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