Chlorine in PDB 4z6w: Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.57 Ang Resolution

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.57 Ang Resolution, PDB code: 4z6w 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)	45.73 / 1.57
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.469, 150.646, 95.996, 90.00, 90.00, 90.00
R / Rfree (%)	13.7 / 16.3

The structure of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol 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 4-Nitrocatechol at 1.57 Ang Resolution (pdb code 4z6w). 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 H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.57 Ang Resolution, PDB code: 4z6w:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol 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 4-Nitrocatechol at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:18.1 occ:0.20 O11 A:4NC403 0.9 15.9 0.8 N9 A:4NC403 2.3 18.8 0.8 NH1 A:ARG243 2.5 22.3 1.0 NH2 A:ARG243 2.9 20.6 1.0 C4 A:4NC403 3.1 16.7 0.8 C3 A:4NC403 3.1 16.1 0.8 CZ A:ARG243 3.1 20.5 1.0 O10 A:4NC403 3.2 21.9 0.8 NH1 A:ARG293 3.4 17.8 1.0 CB A:ARG293 3.4 15.3 1.0 CD A:ARG293 3.4 17.2 1.0 CE1 A:HIS248 3.4 15.2 1.0 CG A:ARG293 3.6 15.9 1.0 ND1 A:HIS248 3.6 14.2 1.0 CH2 A:TRP304 3.8 20.5 1.0 CZ2 A:TRP304 3.9 19.1 1.0 O A:ARG293 3.9 17.2 1.0 OH A:TYR257 3.9 15.5 1.0 CA A:ARG293 3.9 14.3 1.0 C A:ARG293 4.2 14.4 1.0 CZ A:ARG293 4.3 16.4 1.0 NE A:ARG293 4.3 15.5 1.0 C5 A:4NC403 4.4 17.2 0.8 C2 A:4NC403 4.4 16.2 0.8 CZ3 A:TRP304 4.4 21.7 1.0 NE A:ARG243 4.4 20.1 1.0 CE2 A:TRP304 4.6 17.8 1.0 NE2 A:HIS248 4.6 14.2 1.0 CZ A:TYR257 4.8 14.6 1.0 CE2 A:TYR257 4.8 15.6 1.0 CG A:HIS248 4.9 13.7 1.0 O8 A:4NC403 4.9 14.6 0.8

Chlorine binding site 2 out of 3 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol 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 4-Nitrocatechol at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl407 b:12.0 occ:0.30 O11 B:4NC406 0.5 16.4 0.7 N9 B:4NC406 2.0 19.7 0.7 C4 B:4NC406 2.8 16.9 0.7 NH1 B:ARG243 2.9 17.6 1.0 C3 B:4NC406 3.0 14.8 0.7 O10 B:4NC406 3.0 23.3 0.7 NH1 B:ARG293 3.2 14.9 1.0 NH2 B:ARG243 3.2 17.1 1.0 CB B:ARG293 3.4 13.3 1.0 CE1 B:HIS248 3.4 13.9 1.0 CD B:ARG293 3.5 13.7 1.0 CZ B:ARG243 3.5 16.4 1.0 CG B:ARG293 3.5 13.5 1.0 ND1 B:HIS248 3.5 13.4 1.0 CA B:ARG293 3.8 12.5 1.0 O B:ARG293 3.9 14.4 1.0 CH2 B:TRP304 4.0 18.9 1.0 OH B:TYR257 4.0 15.4 1.0 C5 B:4NC406 4.1 16.4 0.7 CZ2 B:TRP304 4.1 17.4 1.0 CZ B:ARG293 4.1 13.6 1.0 C B:ARG293 4.2 13.0 1.0 NE B:ARG293 4.2 13.5 1.0 C2 B:4NC406 4.3 15.1 0.7 NE2 B:HIS248 4.5 12.4 1.0 CZ3 B:TRP304 4.6 19.4 1.0 CG B:HIS248 4.7 12.5 1.0 CE2 B:TRP304 4.8 16.2 1.0 NE B:ARG243 4.8 16.4 1.0 O8 B:4NC406 5.0 11.2 0.7 CZ B:TYR257 5.0 14.1 1.0

Chlorine binding site 3 out of 3 in the Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol 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 3 of Structure of H200N Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Nitrocatechol at 1.57 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl405 b:16.9 occ:0.20 O11 D:4NC404 0.8 15.3 0.8 N9 D:4NC404 2.2 17.1 0.8 NH1 D:ARG243 2.6 21.4 1.0 C4 D:4NC404 2.9 15.6 0.8 C3 D:4NC404 2.9 15.0 0.8 NH2 D:ARG243 3.0 18.6 1.0 O10 D:4NC404 3.2 20.2 0.8 CE1 D:HIS248 3.2 13.2 1.0 CZ D:ARG243 3.3 18.6 1.0 NH1 D:ARG293 3.4 13.6 1.0 ND1 D:HIS248 3.4 12.4 1.0 CB D:ARG293 3.6 13.6 1.0 CD D:ARG293 3.6 14.8 1.0 CG D:ARG293 3.7 14.1 1.0 OH D:TYR257 3.8 14.2 1.0 O D:ARG293 3.9 14.8 1.0 CH2 D:TRP304 3.9 19.5 1.0 CZ2 D:TRP304 4.0 17.6 1.0 CA D:ARG293 4.0 12.4 1.0 C5 D:4NC404 4.2 14.8 0.8 C2 D:4NC404 4.2 14.5 0.8 C D:ARG293 4.3 12.7 1.0 CZ D:ARG293 4.3 13.8 1.0 NE2 D:HIS248 4.4 12.5 1.0 NE D:ARG293 4.4 13.7 1.0 CZ3 D:TRP304 4.5 20.2 1.0 NE D:ARG243 4.6 19.9 1.0 CE2 D:TRP304 4.6 15.3 1.0 CG D:HIS248 4.7 12.1 1.0 CZ D:TYR257 4.7 13.7 1.0 CE2 D:TYR257 4.8 13.3 1.0 O8 D:4NC404 4.9 11.3 0.8

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