Calcium in PDB 4z6s: Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution, PDB code: 4z6s 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)	47.95 / 1.42
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.568, 151.990, 96.356, 90.00, 90.00, 90.00
R / Rfree (%)	12.4 / 16

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Chlorine	(Cl)	3 atoms

The binding sites of Calcium atom in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution (pdb code 4z6s). 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution, PDB code: 4z6s:

Calcium binding site 1 out of 1 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.42 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca402 b:19.0 occ:1.00 OE2 B:GLU185 2.2 27.1 1.0 OD1 B:ASP184 2.3 14.6 1.0 O B:HOH818 2.5 25.1 1.0 CG B:ASP184 3.3 13.8 1.0 CD B:GLU185 3.3 26.3 1.0 OD2 B:ASP184 3.6 13.9 1.0 CG B:GLU185 3.8 25.7 1.0 O B:HOH660 4.1 45.7 1.0 O B:HOH845 4.4 29.1 0.5 OE1 B:GLU185 4.4 35.3 1.0 NE2 B:HIS288 4.5 15.4 1.0 O B:HOH855 4.6 19.9 0.5 O B:HOH845 4.7 25.7 0.5 CB B:GLU185 4.7 18.7 1.0 CB B:ASP184 4.7 12.1 1.0 N B:ASP184 4.7 11.4 1.0 N B:GLU185 4.9 13.9 1.0 CB B:ASP183 4.9 12.7 1.0 OD2 B:ASP183 5.0 17.7 1.0 CA B:ASP184 5.0 12.2 1.0

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