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Calcium in PDB 3ojn: Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution

Enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution

All present enzymatic activity of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution:
1.13.11.15;

Protein crystallography data

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution, PDB code: 3ojn was solved by A.J.Fielding, E.G.Kovaleva, E.R.Farquhar, J.D.Lipscomb, L.Que Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.77 / 1.65
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.542, 151.497, 96.359, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17.7

Other elements in 3ojn:

The structure of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution also contains other interesting chemical elements:

Manganese (Mn) 4 atoms
Chlorine (Cl) 4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution (pdb code 3ojn). 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 Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution, PDB code: 3ojn:

Calcium binding site 1 out of 1 in 3ojn

Go back to Calcium Binding Sites List in 3ojn
Calcium binding site 1 out of 1 in the Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Mn-Substituted Homoprotocatechuate 2,3-Dioxygenase at 1.65 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca366

b:17.1
occ:1.00
 OE2 B:GLU185 2.2 28.4 1.0
OD1 B:ASP184 2.3 15.6 1.0
O B:HOH371 2.3 15.6 1.0
CG B:ASP184 3.3 16.9 1.0
CD B:GLU185 3.4 30.3 1.0
OD2 B:ASP184 3.6 14.8 1.0
CG B:GLU185 3.9 24.6 1.0
O B:HOH458 4.2 24.3 1.0
OE1 B:GLU185 4.4 34.1 1.0
NE2 B:HIS288 4.5 16.0 1.0
N B:ASP184 4.6 15.1 1.0
CB B:ASP184 4.6 15.1 1.0
CB B:GLU185 4.7 20.8 1.0
OD2 B:ASP183 4.8 19.2 1.0
N B:GLU185 4.9 17.6 1.0
CB B:ASP183 4.9 15.2 1.0
CA B:ASP184 5.0 16.0 1.0
CG B:ASP183 5.0 17.6 1.0
CD2 B:HIS288 5.0 13.3 1.0

Reference:

A.J.Fielding, E.G.Kovaleva, E.R.Farquhar, J.D.Lipscomb, L.Que. A Hyperactive Cobalt-Substituted Extradiol-Cleaving Catechol Dioxygenase. J.Biol.Inorg.Chem. V. 16 341 2011.
ISSN: ISSN 0949-8257
PubMed: 21153851
DOI: 10.1007/S00775-010-0732-0
Page generated: Sat Jul 13 15:20:33 2024

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