Chlorine in PDB 5bwh: Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution

The structure of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution, PDB code: 5bwh 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)	29.66 / 1.46
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.414, 151.027, 96.468, 90.00, 90.00, 90.00
R / Rfree (%)	12.2 / 16.1

The structure of Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 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 H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution (pdb code 5bwh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution, PDB code: 5bwh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 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 H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:25.6 occ:1.00 O A:HOH788 2.9 32.1 1.0 NH1 A:ARG243 3.2 15.8 1.0 NH1 A:ARG293 3.2 17.0 1.0 NH2 A:ARG243 3.4 16.1 1.0 CB A:ARG293 3.4 14.4 1.0 CE1 A:HIS248 3.5 15.4 1.0 CG A:ARG293 3.5 14.4 1.0 ND1 A:HIS248 3.5 14.8 1.0 CD A:ARG293 3.6 15.1 1.0 CZ A:ARG243 3.7 14.8 1.0 CA A:ARG293 3.8 13.7 1.0 O A:ARG293 3.9 17.3 1.0 OH A:TYR257 4.0 15.7 1.0 CH2 A:TRP304 4.1 21.3 1.0 C A:ARG293 4.1 14.0 1.0 CZ2 A:TRP304 4.2 17.1 1.0 CZ A:ARG293 4.2 15.8 1.0 NE A:ARG293 4.4 14.7 1.0 O A:HOH795 4.6 32.6 1.0 NE2 A:HIS248 4.7 15.4 1.0 CZ3 A:TRP304 4.7 22.4 1.0 CG A:HIS248 4.8 13.8 1.0 O A:HOH504 4.8 19.8 1.0 CE2 A:TRP304 4.9 17.4 1.0 CZ A:TYR257 4.9 15.6 1.0

Chlorine binding site 2 out of 2 in the Structure of H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 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 H200C Variant of Homoprotocatechuate 2,3-Dioxygenase From B.Fuscum in Complex with Hpca at 1.46 Ang Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl405 b:19.9 occ:1.00 O B:HOH813 3.0 30.3 1.0 NH1 B:ARG293 3.2 15.3 1.0 NH1 B:ARG243 3.2 15.4 1.0 NH2 B:ARG243 3.4 14.8 1.0 CE1 B:HIS248 3.4 13.3 1.0 ND1 B:HIS248 3.5 14.0 1.0 CB B:ARG293 3.5 14.2 1.0 CG B:ARG293 3.5 13.8 1.0 CD B:ARG293 3.6 14.0 1.0 CZ B:ARG243 3.7 14.3 1.0 CA B:ARG293 3.8 13.2 1.0 O B:ARG293 3.8 15.8 1.0 OH B:TYR257 4.0 15.6 1.0 C B:ARG293 4.1 13.2 1.0 CH2 B:TRP304 4.1 18.4 1.0 CZ B:ARG293 4.2 14.7 1.0 CZ2 B:TRP304 4.2 18.6 1.0 NE B:ARG293 4.4 14.3 1.0 NE2 B:HIS248 4.5 14.2 1.0 CG B:HIS248 4.7 12.9 1.0 CZ3 B:TRP304 4.7 23.6 1.0 O B:HOH811 4.7 31.7 1.0 O B:HOH503 4.9 18.8 1.0 CE2 B:TRP304 4.9 16.7 1.0 CZ B:TYR257 4.9 12.8 1.0

K.K.Meier, M.S.Rogers, E.G.Kovaleva, M.M.Mbughuni, E.L.Bominaar, J.D.Lipscomb, E.Munck. A Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization By Mossbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods. Inorg.Chem. V. 54 10269 2015.
ISSN: ISSN 0020-1669
PubMed: 26485328
DOI: 10.1021/ACS.INORGCHEM.5B01576