Chlorine in PDB 4z6r: Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution

The structure of Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution, PDB code: 4z6r 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)	29.43 / 1.70
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.457, 150.482, 95.957, 90.00, 90.00, 90.00
R / Rfree (%)	14.1 / 17.4

The structure of Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 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 H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution (pdb code 4z6r). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution, PDB code: 4z6r:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 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 H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:26.3 occ:1.00 CE1 A:HIS248 3.2 17.1 1.0 NH1 A:ARG243 3.2 20.8 1.0 NH1 A:ARG293 3.3 20.7 1.0 NH2 A:ARG243 3.3 18.6 1.0 ND1 A:HIS248 3.3 15.5 1.0 CB A:ARG293 3.4 16.4 1.0 CG A:ARG293 3.7 17.6 1.0 CD A:ARG293 3.7 19.4 1.0 O A:ARG293 3.7 15.8 1.0 CZ A:ARG243 3.7 18.9 1.0 CA A:ARG293 3.7 15.2 1.0 OH A:TYR257 3.9 17.4 1.0 CH2 A:TRP304 4.1 20.4 1.0 C A:ARG293 4.1 14.8 1.0 CZ2 A:TRP304 4.2 19.1 1.0 CZ A:ARG293 4.3 19.3 1.0 NE2 A:HIS248 4.3 15.9 1.0 NE A:ARG293 4.5 18.1 1.0 CG A:HIS248 4.5 15.3 1.0 CZ3 A:TRP304 4.8 23.8 1.0 O A:HOH503 4.8 21.0 1.0 O A:HOH734 4.8 35.9 1.0 CZ A:TYR257 4.9 17.4 1.0 CE2 A:TYR257 5.0 17.5 1.0 CE2 A:TRP304 5.0 19.1 1.0

Chlorine binding site 2 out of 4 in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 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 H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:19.6 occ:1.00 NH1 B:ARG243 3.1 16.3 1.0 O B:HOH771 3.2 37.7 1.0 NH1 B:ARG293 3.3 16.3 1.0 CE1 B:HIS248 3.3 16.1 1.0 NH2 B:ARG243 3.3 15.8 1.0 ND1 B:HIS248 3.4 16.4 1.0 CB B:ARG293 3.4 13.9 1.0 CG B:ARG293 3.5 14.8 1.0 CD B:ARG293 3.6 15.9 1.0 CZ B:ARG243 3.7 15.2 1.0 O B:ARG293 3.7 14.4 1.0 CA B:ARG293 3.7 13.1 1.0 OH B:TYR257 4.0 17.7 1.0 C B:ARG293 4.1 12.4 1.0 CH2 B:TRP304 4.2 22.1 1.0 CZ2 B:TRP304 4.2 20.5 1.0 CZ B:ARG293 4.3 15.3 1.0 NE B:ARG293 4.4 15.9 1.0 NE2 B:HIS248 4.5 15.3 1.0 CG B:HIS248 4.7 15.3 1.0 CZ3 B:TRP304 4.8 22.8 1.0 O B:HOH503 4.8 20.6 1.0 CE2 B:TRP304 4.9 18.3 1.0 CZ B:TYR257 5.0 15.1 1.0 NE B:ARG243 5.0 14.7 1.0

Chlorine binding site 3 out of 4 in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 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 H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl404 b:9.6 occ:0.20 O11 C:4SX403 0.4 22.5 0.8 S9 C:4SX403 1.8 35.2 0.8 O10 C:4SX403 2.6 34.9 0.8 C4 C:4SX403 2.8 26.9 0.8 C3 C:4SX403 2.9 22.9 0.8 O12 C:4SX403 2.9 30.6 0.8 NH1 C:ARG243 3.0 21.0 1.0 NH1 C:ARG293 3.2 19.1 1.0 NH2 C:ARG243 3.3 19.3 1.0 CE1 C:HIS248 3.4 16.4 1.0 ND1 C:HIS248 3.5 16.4 1.0 CB C:ARG293 3.6 18.0 1.0 CZ C:ARG243 3.6 18.8 1.0 CG C:ARG293 3.6 19.7 1.0 CD C:ARG293 3.7 19.0 1.0 CH2 C:TRP304 3.9 21.8 1.0 CA C:ARG293 3.9 18.6 1.0 O C:ARG293 3.9 16.8 1.0 OH C:TYR257 4.0 16.1 1.0 CZ2 C:TRP304 4.1 19.7 1.0 C5 C:4SX403 4.1 19.4 0.8 C2 C:4SX403 4.2 22.3 0.8 CZ C:ARG293 4.2 19.6 1.0 C C:ARG293 4.2 18.9 1.0 NE C:ARG293 4.4 18.6 1.0 NE2 C:HIS248 4.5 15.8 1.0 CZ3 C:TRP304 4.6 21.4 1.0 CG C:HIS248 4.7 14.2 1.0 O8 C:4SX403 4.8 16.5 0.8 CE2 C:TRP304 4.8 17.5 1.0 NE C:ARG243 4.9 18.8 1.0 CZ C:TYR257 4.9 15.2 1.0

Chlorine binding site 4 out of 4 in the Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of H200E Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with 4-Sulfonyl Catechol at 1.70 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl403 b:24.9 occ:1.00 NH1 D:ARG243 3.2 22.4 1.0 NH2 D:ARG243 3.2 17.5 1.0 CE1 D:HIS248 3.3 15.5 1.0 NH1 D:ARG293 3.3 16.1 1.0 ND1 D:HIS248 3.3 15.3 1.0 CB D:ARG293 3.5 14.9 1.0 CG D:ARG293 3.5 16.2 1.0 O D:HOH741 3.5 34.7 1.0 CD D:ARG293 3.6 16.9 1.0 CZ D:ARG243 3.6 18.6 1.0 O D:ARG293 3.7 13.4 1.0 CA D:ARG293 3.8 13.5 1.0 OH D:TYR257 4.0 15.8 1.0 C D:ARG293 4.1 13.6 1.0 CH2 D:TRP304 4.1 20.7 1.0 CZ2 D:TRP304 4.3 18.5 1.0 CZ D:ARG293 4.3 16.9 1.0 NE D:ARG293 4.4 15.9 1.0 NE2 D:HIS248 4.4 13.8 1.0 CG D:HIS248 4.6 14.2 1.0 CZ3 D:TRP304 4.7 21.2 1.0 O D:HOH507 4.9 22.4 1.0 CZ D:TYR257 4.9 14.4 1.0 CE2 D:TRP304 5.0 15.9 1.0 NE D:ARG243 5.0 17.6 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