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Calcium in PDB 4asm: Crystal Structure of the Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans

Enzymatic activity of Crystal Structure of the Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans

All present enzymatic activity of Crystal Structure of the Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans:
3.2.1.81;

Protein crystallography data

The structure of Crystal Structure of the Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans, PDB code: 4asm was solved by J.H.Hehemann, G.Correc, T.Bernard, G.Michel, M.Czjzek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.80 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.247, 77.268, 83.695, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 19

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans (pdb code 4asm). 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 Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans, PDB code: 4asm:

Calcium binding site 1 out of 1 in 4asm

Go back to Calcium Binding Sites List in 4asm
Calcium binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans


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 Catalytic Domain of Beta-Agarase D From Zobellia Galactanivorans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1359

b:9.0
occ:1.00
 OD2 B:ASP4 2.3 14.1 1.0
OD1 B:ASP349 2.4 10.1 1.0
O B:GLY84 2.4 8.8 1.0
O B:ASP29 2.4 8.3 1.0
O B:HOH2017 2.4 13.1 1.0
O B:ASP349 2.5 7.7 1.0
OD1 B:ASN31 2.5 11.6 1.0
C B:GLY84 3.4 8.7 1.0
CG B:ASN31 3.4 11.2 1.0
C B:ASP349 3.5 7.2 1.0
CG B:ASP349 3.5 8.4 1.0
CG B:ASP4 3.5 13.3 1.0
C B:ASP29 3.6 8.2 1.0
ND2 B:ASN31 3.8 11.8 1.0
CA B:ASP349 3.9 6.8 1.0
CA B:GLY84 3.9 9.1 1.0
O B:PHE30 4.2 9.6 1.0
OD1 B:ASP4 4.2 13.4 1.0
C B:PHE30 4.3 9.4 1.0
O B:HOH2229 4.3 25.6 1.0
CB B:ASP349 4.3 7.0 1.0
CB B:ASP29 4.3 8.7 1.0
CA B:ASP29 4.4 8.7 1.0
OD2 B:ASP349 4.5 10.3 1.0
O B:HOH2584 4.5 33.2 1.0
N B:PHE30 4.5 7.6 1.0
CB B:PHE30 4.6 8.4 1.0
CB B:ASP4 4.6 11.1 1.0
N B:ASN85 4.6 8.2 1.0
N B:TRP350 4.6 6.8 1.0
O B:HOH2585 4.6 46.0 1.0
CA B:PHE30 4.7 8.3 1.0
N B:ASN31 4.7 10.9 1.0
CB B:ASN31 4.8 11.8 1.0
CB B:TRP350 4.9 7.2 1.0
CA B:ASN31 4.9 11.8 1.0
CA B:ASN85 5.0 7.2 1.0

Reference:

J.H.Hehemann, G.Correc, F.Thomas, T.Bernard, T.Barbeyron, M.Jam, W.Helbert, G.Michel, M.Czjzek. Biochemical and Structural Characterization of the Complex Agarolytic Enzyme System From the Marine Bacterium Zobellia Galactanivorans. J.Biol.Chem. V. 287 30571 2012.
ISSN: ISSN 0021-9258
PubMed: 22778272
DOI: 10.1074/JBC.M112.377184
Page generated: Sat Jul 13 22:18:06 2024

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