Bromine in PDB 4hsx: Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol

All present enzymatic activity of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol:
1.11.1.7;

The structure of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol, PDB code: 4hsx was solved by M.K.Thompson, A.Plummer, S.Franzen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.34 / 1.12
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.241, 67.441, 69.338, 90.00, 90.00, 90.00
R / Rfree (%)	12.6 / 15

The structure of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Bromine atom in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol (pdb code 4hsx). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol, PDB code: 4hsx:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol within 5.0Å range: probe atom residue distance (Å) B Occ A:Br206 b:12.0 occ:0.35 BR4 A:BML206 0.0 12.0 0.3 C4 A:BML206 1.7 6.4 0.3 CE2 A:PHE100 2.7 16.2 1.0 C5 A:BML206 2.8 8.2 0.3 O A:HOH512 2.8 12.9 1.0 C3 A:BML206 2.9 6.6 0.3 CZ A:PHE100 3.2 18.1 1.0 CD1 A:PHE21 3.5 10.9 1.0 CE1 A:PHE21 3.6 10.2 1.0 CD2 A:PHE100 3.7 14.1 1.0 C1C A:HEM201 3.8 8.6 1.0 CG1 A:VAL59 3.9 8.2 1.0 NC A:HEM201 3.9 7.9 1.0 CE1 A:HIS55 4.0 5.1 0.4 CHC A:HEM201 4.1 7.9 1.0 C2 A:BML206 4.2 8.6 0.3 C6 A:BML206 4.2 7.9 0.3 C2C A:HEM201 4.2 9.6 1.0 C4C A:HEM201 4.3 8.4 1.0 C4B A:HEM201 4.4 7.5 1.0 CZ A:PHE35 4.4 9.8 1.0 CG2 A:VAL59 4.4 8.7 1.0 CE1 A:PHE100 4.5 19.9 1.0 C3C A:HEM201 4.5 9.9 1.0 NB A:HEM201 4.6 7.3 1.0 FE A:HEM201 4.6 7.7 1.0 CB A:VAL59 4.7 7.2 1.0 NE2 A:HIS55 4.7 7.9 0.4 C1 A:BML206 4.7 8.6 0.3 CZ A:PHE21 4.8 6.7 1.0 CG A:PHE21 4.8 5.9 1.0 CE2 A:PHE35 4.8 10.9 1.0 CG A:PHE100 4.9 10.1 1.0

Bromine binding site 2 out of 2 in the Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of the L100F Mutant of Dehaloperoxidase-Hemoglobin A From Amphitrite Ornata with 4-Bromophenol within 5.0Å range: probe atom residue distance (Å) B Occ B:Br203 b:12.8 occ:0.40 BR4 B:BML203 0.0 12.8 0.4 C4 B:BML203 1.8 7.9 0.4 C3 B:BML203 2.7 8.3 0.4 C5 B:BML203 2.7 7.3 0.4 CD1 B:PHE100 3.7 13.1 1.0 CE1 B:PHE100 3.7 14.6 1.0 O B:HOH494 3.7 10.1 0.5 CD1 B:PHE21 3.8 7.4 1.0 CE1 B:PHE21 3.9 8.7 1.0 C1C B:HEM201 3.9 8.7 1.0 CG1 B:VAL59 4.0 7.2 1.0 CHC B:HEM201 4.0 9.9 1.0 C2 B:BML203 4.0 7.5 0.4 C6 B:BML203 4.1 8.6 0.4 C2C B:HEM201 4.1 10.4 1.0 NC B:HEM201 4.3 8.6 1.0 CG B:PHE100 4.4 11.2 1.0 CZ B:PHE100 4.5 15.1 1.0 C4B B:HEM201 4.5 8.0 1.0 CMC B:HEM201 4.5 12.5 1.0 C1 B:BML203 4.6 7.6 0.4 C3C B:HEM201 4.6 10.6 1.0 C4C B:HEM201 4.7 9.7 1.0 CG B:PHE21 4.8 6.3 1.0 CZ B:PHE21 4.9 8.3 1.0 CG2 B:VAL59 4.9 8.7 1.0 NB B:HEM201 4.9 7.7 1.0 CD2 B:PHE24 4.9 7.5 1.0 CB B:VAL59 4.9 6.2 1.0 CE2 B:PHE24 5.0 8.8 1.0

A.Plummer, M.K.Thompson, S.Franzen. Role of Polarity of the Distal Pocket in the Control of Inhibitor Binding in Dehaloperoxidase-Hemoglobin. Biochemistry V. 52 2218 2013.
ISSN: ISSN 0006-2960
PubMed: 23480794
DOI: 10.1021/BI301509R