Chlorine in PDB 4z6q: Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution, PDB code: 4z6q 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)	45.69 / 1.57
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.507, 150.077, 95.936, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 16.5

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Calcium	(Ca)	1 atom

The binding sites of Chlorine atom in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution (pdb code 4z6q). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution, PDB code: 4z6q:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:23.0 occ:1.00 NH1 A:ARG243 3.2 14.7 1.0 NH1 A:ARG293 3.2 15.9 1.0 NH2 A:ARG243 3.4 14.3 1.0 CE1 A:HIS248 3.4 15.5 1.0 CB A:ARG293 3.4 14.4 1.0 ND1 A:HIS248 3.4 14.4 1.0 CG A:ARG293 3.6 14.5 1.0 CD A:ARG293 3.6 15.3 1.0 CA A:ARG293 3.7 13.2 1.0 CZ A:ARG243 3.7 13.7 1.0 O A:ARG293 3.9 15.8 1.0 C A:ARG293 4.1 13.5 1.0 OH A:TYR257 4.1 16.2 1.0 CH2 A:TRP304 4.2 18.0 1.0 CZ A:ARG293 4.2 14.8 1.0 CZ2 A:TRP304 4.2 16.4 1.0 NE A:ARG293 4.3 14.7 1.0 NE2 A:HIS248 4.6 14.8 1.0 CG A:HIS248 4.7 14.0 1.0 O A:HOH823 4.7 31.1 1.0 O A:HOH506 4.8 19.9 1.0 CZ3 A:TRP304 4.8 18.4 1.0 CE2 A:TRP304 5.0 15.9 1.0

Chlorine binding site 2 out of 2 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:18.1 occ:1.00 O B:HOH823 3.1 39.8 1.0 NH1 B:ARG243 3.2 14.3 1.0 NH1 B:ARG293 3.2 14.0 1.0 NH2 B:ARG243 3.3 13.9 1.0 CE1 B:HIS248 3.3 14.1 1.0 ND1 B:HIS248 3.4 14.2 1.0 CB B:ARG293 3.5 12.9 1.0 CG B:ARG293 3.5 12.8 1.0 CD B:ARG293 3.6 13.0 1.0 CZ B:ARG243 3.7 13.5 1.0 CA B:ARG293 3.8 12.8 1.0 O B:ARG293 3.8 14.9 1.0 OH B:TYR257 4.1 16.0 1.0 C B:ARG293 4.1 12.5 1.0 CH2 B:TRP304 4.2 17.7 1.0 CZ B:ARG293 4.2 13.1 1.0 CZ2 B:TRP304 4.3 18.2 1.0 NE B:ARG293 4.3 12.9 1.0 CG2 B:VAL250 4.4 16.7 0.5 NE2 B:HIS248 4.5 14.0 1.0 CG B:HIS248 4.6 12.8 1.0 CZ3 B:TRP304 4.7 18.9 1.0 O B:HOH824 4.8 30.7 1.0 CE2 B:TRP304 4.9 16.4 1.0 O B:HOH508 4.9 19.4 1.0 NE B:ARG243 5.0 13.3 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