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Calcium in PDB 2ig9: Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.

Enzymatic activity of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.

All present enzymatic activity of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.:
1.13.11.15;

Protein crystallography data

The structure of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup., PDB code: 2ig9 was solved by E.G.Kovaleva, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.08 / 1.90
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.445, 152.802, 99.714, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 23.4

Other elements in 2ig9:

The structure of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Chlorine (Cl) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. (pdb code 2ig9). 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 Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup., PDB code: 2ig9:

Calcium binding site 1 out of 1 in 2ig9

Go back to Calcium Binding Sites List in 2ig9
Calcium binding site 1 out of 1 in the Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of A Full-Length Homoprotocatechuate 2,3-Dioxygenase From B. Fuscum in A New Spacegroup. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca601

b:24.0
occ:1.00
OE2 B:GLU185 2.3 29.2 1.0
OD1 B:ASP184 2.4 15.5 1.0
O B:HOH813 2.6 33.3 1.0
CG B:ASP184 3.4 19.4 1.0
CD B:GLU185 3.4 30.9 1.0
OD2 B:ASP184 3.6 19.8 1.0
CG B:GLU185 3.9 26.3 1.0
O B:HOH888 4.1 47.9 1.0
NE2 B:HIS288 4.3 18.4 1.0
O B:HOH1041 4.4 36.5 1.0
O B:HOH1101 4.4 40.3 1.0
OE1 B:GLU185 4.5 32.0 1.0
N B:ASP184 4.6 19.7 1.0
CB B:ASP184 4.7 20.2 1.0
CB B:GLU185 4.8 22.4 1.0
N B:GLU185 4.8 21.7 1.0
CB B:ASP183 4.8 18.4 1.0
CD2 B:HIS288 5.0 17.3 1.0
OD2 B:ASP183 5.0 22.1 1.0
CG B:ASP183 5.0 19.1 1.0

Reference:

E.G.Kovaleva, J.D.Lipscomb. Crystal Structures of FE2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates Science V. 316 453 2007.
ISSN: ISSN 0036-8075
PubMed: 17446402
DOI: 10.1126/SCIENCE.1134697
Page generated: Fri Jul 12 13:05:27 2024

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