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Calcium in PDB 4z6o: Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 Ang Resolution

Protein crystallography data

The structure of Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 Ang Resolution, PDB code: 4z6o 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) 47.82 / 1.63
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 110.314, 150.478, 95.972, 90.00, 90.00, 90.00
R / Rfree (%) 13.8 / 16.7

Other elements in 4z6o:

The structure of Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 Ang Resolution also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 Ang Resolution (pdb code 4z6o). 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 H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 Ang Resolution, PDB code: 4z6o:

Calcium binding site 1 out of 1 in 4z6o

Go back to Calcium Binding Sites List in 4z6o
Calcium binding site 1 out of 1 in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 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 H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.63 Ang Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca402

b:15.1
occ:1.00
OE2 B:GLU185 2.2 25.7 1.0
OD1 B:ASP184 2.3 15.5 1.0
O B:HOH741 2.4 18.4 1.0
CG B:ASP184 3.3 15.2 1.0
CD B:GLU185 3.3 25.1 1.0
OD2 B:ASP184 3.6 13.9 1.0
CG B:GLU185 3.8 22.9 1.0
O B:HOH683 4.1 33.5 1.0
OE1 B:GLU185 4.4 27.8 1.0
NE2 B:HIS288 4.4 15.0 1.0
O B:HOH828 4.5 38.3 1.0
CB B:ASP184 4.6 14.2 1.0
N B:ASP184 4.6 13.8 1.0
CB B:GLU185 4.7 20.3 1.0
OD2 B:ASP183 4.7 17.6 1.0
N B:GLU185 4.9 15.8 1.0
CB B:ASP183 4.9 14.9 1.0
CD2 B:HIS288 5.0 13.9 1.0
CA B:ASP184 5.0 15.2 1.0
CG B:ASP183 5.0 16.0 1.0

Reference:

E.G.Kovaleva, M.S.Rogers, J.D.Lipscomb. Structural Basis For Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200. Biochemistry V. 54 5329 2015.
ISSN: ISSN 0006-2960
PubMed: 26267790
DOI: 10.1021/ACS.BIOCHEM.5B00709
Page generated: Sat Dec 12 05:14:44 2020

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