Chlorine in PDB 4z6v: Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.37 Ang Resolution

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.37 Ang Resolution, PDB code: 4z6v 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)	40.35 / 1.37
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.180, 150.635, 96.103, 90.00, 90.00, 90.00
R / Rfree (%)	11.9 / 15.7

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.37 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-Nitrocatechol at 1.37 Ang Resolution (pdb code 4z6v). 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-Nitrocatechol at 1.37 Ang Resolution, PDB code: 4z6v:
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-Nitrocatechol at 1.37 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-Nitrocatechol at 1.37 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:15.9 occ:1.00 O A:HOH801 3.1 33.0 1.0 NH1 A:ARG243 3.2 14.0 1.0 NH1 A:ARG293 3.2 11.8 1.0 CE1 A:HIS248 3.3 10.8 1.0 NH2 A:ARG243 3.3 12.1 1.0 ND1 A:HIS248 3.4 10.7 1.0 CB A:ARG293 3.4 10.3 1.0 CG A:ARG293 3.5 10.7 1.0 CD A:ARG293 3.6 11.6 1.0 CZ A:ARG243 3.7 12.5 1.0 CA A:ARG293 3.7 10.0 1.0 O A:ARG293 3.8 11.1 1.0 OH A:TYR257 3.9 11.9 1.0 C A:ARG293 4.1 9.9 1.0 CH2 A:TRP304 4.1 15.0 1.0 CZ2 A:TRP304 4.2 13.4 1.0 CZ A:ARG293 4.2 11.1 1.0 NE A:ARG293 4.4 11.4 1.0 NE2 A:HIS248 4.4 10.4 1.0 CG A:HIS248 4.6 11.3 1.0 O A:HOH506 4.6 15.1 1.0 CZ3 A:TRP304 4.8 17.1 1.0 CZ A:TYR257 4.9 9.5 1.0 O A:HOH828 4.9 23.7 1.0 CE2 A:TRP304 4.9 11.6 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-Nitrocatechol at 1.37 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-Nitrocatechol at 1.37 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:13.7 occ:1.00 O B:HOH845 3.1 31.0 1.0 NH1 B:ARG293 3.2 11.6 1.0 NH1 B:ARG243 3.2 11.5 1.0 CE1 B:HIS248 3.3 10.0 1.0 NH2 B:ARG243 3.3 11.5 1.0 ND1 B:HIS248 3.4 10.1 1.0 CB B:ARG293 3.5 9.3 1.0 CG B:ARG293 3.6 10.2 1.0 CD B:ARG293 3.7 10.7 1.0 CZ B:ARG243 3.7 11.0 1.0 O B:ARG293 3.7 10.7 1.0 CA B:ARG293 3.8 9.4 1.0 OH B:TYR257 4.0 12.1 1.0 C B:ARG293 4.1 9.7 1.0 CH2 B:TRP304 4.2 13.2 1.0 CZ2 B:TRP304 4.2 12.9 1.0 CZ B:ARG293 4.2 11.3 1.0 NE2 B:HIS248 4.4 10.2 1.0 NE B:ARG293 4.4 11.0 1.0 O B:HOH765 4.4 28.6 1.0 CG B:HIS248 4.6 9.6 1.0 O B:HOH509 4.7 12.8 1.0 CZ3 B:TRP304 4.8 14.8 1.0 CE2 B:TRP304 4.9 12.9 1.0 CZ B:TYR257 4.9 10.4 1.0 O B:HOH853 5.0 23.4 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-Nitrocatechol at 1.37 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-Nitrocatechol at 1.37 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl403 b:13.3 occ:1.00 O D:HOH827 3.1 36.6 1.0 NH1 D:ARG243 3.2 11.8 1.0 NH1 D:ARG293 3.2 10.7 1.0 CE1 D:HIS248 3.3 10.1 1.0 NH2 D:ARG243 3.3 10.7 1.0 ND1 D:HIS248 3.4 9.0 1.0 CB D:ARG293 3.5 9.0 1.0 CG D:ARG293 3.5 9.7 1.0 CD D:ARG293 3.6 11.2 1.0 CZ D:ARG243 3.7 10.5 1.0 O D:ARG293 3.8 10.2 1.0 CA D:ARG293 3.8 8.9 1.0 OH D:TYR257 4.0 11.5 1.0 CH2 D:TRP304 4.1 13.3 1.0 C D:ARG293 4.1 9.7 1.0 CZ2 D:TRP304 4.2 11.7 1.0 CZ D:ARG293 4.2 10.0 1.0 NE D:ARG293 4.4 9.5 1.0 NE2 D:HIS248 4.4 9.6 1.0 CG D:HIS248 4.6 8.4 1.0 O D:HOH504 4.7 13.0 1.0 CZ3 D:TRP304 4.7 13.8 1.0 CE2 D:TRP304 4.9 10.1 1.0 CZ D:TYR257 4.9 8.9 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