Chlorine 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
Calcium	(Ca)	1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total 3 binding sites of Chlorine where 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:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 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 Chlorine with other atoms in the Cl 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 A:Cl402 b:21.0 occ:1.00 NH1 A:ARG243 3.1 15.7 1.0 NH1 A:ARG293 3.3 12.7 1.0 NH2 A:ARG243 3.3 15.1 1.0 CE1 A:HIS248 3.3 10.9 1.0 ND1 A:HIS248 3.4 13.2 1.0 CB A:ARG293 3.4 11.4 1.0 CG A:ARG293 3.5 12.1 1.0 CD A:ARG293 3.6 12.2 1.0 CZ A:ARG243 3.6 14.1 1.0 O A:ARG293 3.7 12.0 1.0 CA A:ARG293 3.7 9.5 1.0 OH A:TYR257 4.0 14.3 1.0 C A:ARG293 4.1 10.4 1.0 CH2 A:TRP304 4.1 17.2 1.0 CZ2 A:TRP304 4.2 14.5 1.0 CZ A:ARG293 4.3 13.0 1.0 NE A:ARG293 4.4 12.6 1.0 NE2 A:HIS248 4.5 12.1 1.0 CG A:HIS248 4.6 11.3 1.0 CZ3 A:TRP304 4.7 17.7 1.0 O A:HOH501 4.8 15.3 1.0 CE2 A:TRP304 4.9 12.7 1.0 NE A:ARG243 5.0 14.3 1.0 CZ A:TYR257 5.0 14.2 1.0

Chlorine binding site 2 out of 3 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 Chlorine with other atoms in the Cl binding site number 2 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:Cl403 b:16.1 occ:1.00 O B:HOH840 3.0 50.0 1.0 NH1 B:ARG243 3.2 13.2 1.0 NH1 B:ARG293 3.3 13.2 1.0 NH2 B:ARG243 3.3 13.5 1.0 CE1 B:HIS248 3.3 11.8 1.0 ND1 B:HIS248 3.4 10.6 1.0 CB B:ARG293 3.4 11.0 1.0 CG B:ARG293 3.5 10.9 1.0 CD B:ARG293 3.6 11.8 1.0 CZ B:ARG243 3.7 12.4 1.0 O B:ARG293 3.8 11.4 1.0 CA B:ARG293 3.8 10.1 1.0 OH B:TYR257 4.0 12.3 1.0 C B:ARG293 4.1 10.9 1.0 CH2 B:TRP304 4.2 15.7 1.0 CZ2 B:TRP304 4.2 13.5 1.0 CZ B:ARG293 4.3 12.1 1.0 NE B:ARG293 4.4 12.0 1.0 NE2 B:HIS248 4.4 12.2 1.0 CG B:HIS248 4.6 10.1 1.0 CZ3 B:TRP304 4.7 17.5 1.0 O B:HOH507 4.7 13.6 1.0 CE2 B:TRP304 4.8 12.2 1.0 CZ B:TYR257 5.0 11.7 1.0

Chlorine binding site 3 out of 3 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 Chlorine with other atoms in the Cl binding site number 3 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 D:Cl402 b:8.0 occ:0.20 O11 D:4SX403 0.7 14.2 0.8 S9 D:4SX403 2.1 17.8 0.8 NH1 D:ARG243 2.7 15.7 1.0 O10 D:4SX403 2.7 17.4 0.8 C3 D:4SX403 2.9 13.4 0.8 C4 D:4SX403 3.0 15.4 0.8 NH2 D:ARG243 3.2 14.3 1.0 O12 D:4SX403 3.3 15.8 0.8 CE1 D:HIS248 3.4 11.8 1.0 NH1 D:ARG293 3.4 13.6 1.0 CZ D:ARG243 3.4 13.0 1.0 CB D:ARG293 3.5 11.1 1.0 ND1 D:HIS248 3.5 10.7 1.0 CD D:ARG293 3.6 12.8 1.0 CG D:ARG293 3.7 11.8 1.0 CH2 D:TRP304 3.8 18.6 1.0 O D:ARG293 3.9 11.3 1.0 CZ2 D:TRP304 3.9 16.3 1.0 CA D:ARG293 3.9 11.2 1.0 OH D:TYR257 4.0 13.3 1.0 C2 D:4SX403 4.2 15.3 0.8 C D:ARG293 4.2 10.0 1.0 C5 D:4SX403 4.3 13.2 0.8 CZ D:ARG293 4.3 12.4 1.0 CZ3 D:TRP304 4.3 20.4 1.0 NE D:ARG293 4.4 12.2 1.0 NE2 D:HIS248 4.5 10.5 1.0 CE2 D:TRP304 4.7 13.4 1.0 NE D:ARG243 4.7 13.3 1.0 CG D:HIS248 4.8 10.5 1.0 O8 D:4SX403 4.8 10.4 0.8 CZ D:TYR257 4.9 12.8 1.0 CE2 D:TYR257 5.0 12.4 1.0 CE3 D:TRP304 5.0 17.0 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