Chlorine in PDB 4z6m: Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 Ang Resolution

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 Ang Resolution, PDB code: 4z6m 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)	48.09 / 1.35
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.485, 152.089, 96.188, 90.00, 90.00, 90.00
R / Rfree (%)	11.2 / 14

The structure of Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 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 at 1.35 Ang Resolution (pdb code 4z6m). 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 Ang Resolution, PDB code: 4z6m:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 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 at 1.35 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:10.9 occ:1.00 O A:HOH843 3.1 21.6 1.0 NH1 A:ARG243 3.2 8.7 1.0 NH1 A:ARG293 3.2 8.4 1.0 CE1 A:HIS248 3.3 8.0 1.0 NH2 A:ARG243 3.3 8.3 1.0 ND1 A:HIS248 3.4 7.9 1.0 CB A:ARG293 3.5 7.8 1.0 CG A:ARG293 3.5 8.1 1.0 CD A:ARG293 3.6 8.1 1.0 CZ A:ARG243 3.7 8.2 1.0 O A:ARG293 3.8 8.1 1.0 CA A:ARG293 3.8 6.9 1.0 OH A:TYR257 3.9 9.0 1.0 CH2 A:TRP304 4.1 11.3 1.0 C A:ARG293 4.1 7.1 1.0 CZ2 A:TRP304 4.2 9.3 1.0 CZ A:ARG293 4.2 8.6 1.0 NE A:ARG293 4.4 8.3 1.0 NE2 A:HIS248 4.4 8.1 1.0 CG A:HIS248 4.6 7.6 1.0 O A:HOH512 4.7 10.3 1.0 CZ3 A:TRP304 4.7 11.3 1.0 CE2 A:TRP304 4.8 8.2 1.0 CZ A:TYR257 4.9 7.3 1.0

Chlorine binding site 2 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 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 at 1.35 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl403 b:10.0 occ:1.00 NH1 B:ARG243 3.2 7.7 1.0 O B:HOH863 3.2 22.2 1.0 NH1 B:ARG293 3.2 6.9 1.0 CE1 B:HIS248 3.3 6.7 1.0 NH2 B:ARG243 3.3 8.0 1.0 ND1 B:HIS248 3.4 7.2 1.0 CB B:ARG293 3.5 6.5 1.0 CG B:ARG293 3.5 6.8 1.0 CD B:ARG293 3.6 6.9 1.0 CZ B:ARG243 3.7 7.0 1.0 O B:ARG293 3.8 7.6 1.0 CA B:ARG293 3.8 6.1 1.0 OH B:TYR257 4.0 7.4 1.0 C B:ARG293 4.1 6.3 1.0 CH2 B:TRP304 4.1 9.2 1.0 CZ2 B:TRP304 4.2 8.2 1.0 CZ B:ARG293 4.2 6.5 1.0 NE B:ARG293 4.3 6.9 1.0 NE2 B:HIS248 4.4 7.3 1.0 CG B:HIS248 4.6 7.2 1.0 O B:HOH507 4.7 8.9 1.0 CZ3 B:TRP304 4.7 9.8 1.0 CE2 B:TRP304 4.8 7.0 1.0 CZ B:TYR257 4.9 6.6 1.0

Chlorine binding site 3 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 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 at 1.35 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl402 b:13.2 occ:1.00 NH1 C:ARG243 3.2 10.1 1.0 NH1 C:ARG293 3.2 10.9 1.0 O C:HOH829 3.2 28.9 1.0 CE1 C:HIS248 3.2 9.7 1.0 NH2 C:ARG243 3.3 9.7 1.0 ND1 C:HIS248 3.4 9.4 1.0 CB C:ARG293 3.5 9.2 1.0 CG C:ARG293 3.6 9.9 1.0 CD C:ARG293 3.6 9.9 1.0 CZ C:ARG243 3.7 10.1 1.0 O C:ARG293 3.7 9.4 1.0 CA C:ARG293 3.8 9.3 1.0 OH C:TYR257 4.0 10.2 1.0 C C:ARG293 4.1 8.2 1.0 CH2 C:TRP304 4.1 12.8 1.0 CZ2 C:TRP304 4.2 10.9 1.0 CZ C:ARG293 4.2 9.5 1.0 NE C:ARG293 4.4 9.7 1.0 NE2 C:HIS248 4.4 8.8 1.0 CG C:HIS248 4.6 8.9 1.0 CZ3 C:TRP304 4.7 13.4 1.0 O C:HOH508 4.7 11.1 1.0 CE2 C:TRP304 4.8 9.2 1.0 CZ C:TYR257 4.9 8.0 1.0

Chlorine binding site 4 out of 4 in the Structure of H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 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 H200Q Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum at 1.35 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl402 b:11.4 occ:1.00 NH1 D:ARG243 3.2 8.7 1.0 O D:HOH835 3.2 24.0 1.0 NH1 D:ARG293 3.2 9.5 1.0 CE1 D:HIS248 3.3 8.3 1.0 NH2 D:ARG243 3.3 8.8 1.0 ND1 D:HIS248 3.4 7.5 1.0 CB D:ARG293 3.5 7.8 1.0 CG D:ARG293 3.6 8.5 1.0 CD D:ARG293 3.7 8.5 1.0 CZ D:ARG243 3.7 8.3 1.0 O D:ARG293 3.7 8.5 1.0 CA D:ARG293 3.8 7.4 1.0 OH D:TYR257 3.9 8.9 1.0 C D:ARG293 4.1 7.3 1.0 CH2 D:TRP304 4.1 11.3 1.0 CZ2 D:TRP304 4.2 9.6 1.0 CZ D:ARG293 4.2 8.5 1.0 NE D:ARG293 4.4 9.0 1.0 NE2 D:HIS248 4.4 7.8 1.0 CG D:HIS248 4.6 7.3 1.0 O D:HOH506 4.7 10.0 1.0 CZ3 D:TRP304 4.7 12.5 1.0 CE2 D:TRP304 4.8 9.3 1.0 CZ D:TYR257 4.9 7.8 1.0 CE2 D:TYR257 5.0 7.8 1.0 NE D:ARG243 5.0 8.0 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