Bromine in PDB 6ju1: P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate

All present enzymatic activity of P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate:
1.14.13.2;

The structure of P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate, PDB code: 6ju1 was solved by M.Yato, T.Arakawa, C.Yamada, S.Fushinobu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.13 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	70.866, 145.901, 86.421, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 18.6

The binding sites of Bromine atom in the P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate (pdb code 6ju1). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate, PDB code: 6ju1:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br409 b:20.1 occ:1.00 O A:HOH613 3.1 18.8 1.0 C10 A:FAD401 3.3 15.4 1.0 N A:GLY298 3.3 16.0 1.0 N10 A:FAD401 3.4 15.9 1.0 CA A:PRO293 3.4 17.7 1.0 N A:LYS297 3.5 15.8 1.0 N1 A:FAD401 3.5 15.2 1.0 O A:HOH607 3.5 20.7 1.0 C1' A:FAD401 3.7 15.1 1.0 CG2 A:VAL291 3.8 14.8 1.0 C4X A:FAD401 3.8 17.2 1.0 C9A A:FAD401 3.8 14.8 1.0 CA A:ALA296 3.9 17.0 1.0 CB A:PRO293 4.0 20.0 1.0 C A:ALA296 4.0 17.2 1.0 CA A:GLY298 4.1 15.5 1.0 N A:ALA296 4.1 17.8 1.0 N A:PRO293 4.1 16.9 1.0 C2 A:FAD401 4.1 17.2 1.0 C5X A:FAD401 4.2 16.8 1.0 O A:PRO292 4.2 15.5 1.0 N5 A:FAD401 4.2 16.1 1.0 O A:PRO293 4.2 15.8 1.0 C A:PRO293 4.3 17.2 1.0 C A:LYS297 4.3 16.1 1.0 O A:VAL291 4.3 15.6 1.0 CG A:PRO293 4.4 22.3 1.0 CA A:LYS297 4.4 16.4 1.0 C A:PRO292 4.4 14.7 1.0 C4 A:FAD401 4.5 17.2 1.0 N3 A:FAD401 4.6 17.6 1.0 C9 A:FAD401 4.6 17.5 1.0 O2 A:FAD401 4.8 17.2 1.0 CD A:PRO293 4.9 19.8 1.0 C A:VAL291 4.9 14.1 1.0 CB A:VAL291 4.9 15.3 1.0

Bromine binding site 2 out of 2 in the P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of P-Hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate within 5.0Å range: probe atom residue distance (Å) B Occ A:Br410 b:31.8 occ:1.00 O A:ILE43 2.3 32.5 1.0 C A:ILE43 3.2 25.8 1.0 NE A:ARG214 3.5 19.8 1.0 N A:THR103 3.5 17.3 1.0 N A:GLN102 3.5 17.6 1.0 O A:HOH829 3.5 17.9 1.0 CG2 A:THR103 3.5 29.2 1.0 O A:ALA45 3.6 17.9 1.0 CA A:ILE43 3.6 20.7 1.0 OG1 A:THR103 3.7 27.1 1.0 CG2 A:ILE43 3.7 23.0 1.0 CA A:GLY101 3.8 18.8 1.0 C A:GLY101 3.9 19.0 1.0 NH2 A:ARG214 4.0 19.3 1.0 CB A:THR103 4.0 23.6 1.0 O A:ARG44 4.1 18.3 1.0 CZ A:ARG214 4.2 17.6 1.0 N A:ARG44 4.2 26.0 1.0 C A:ARG44 4.2 18.9 1.0 CA A:GLN102 4.2 17.6 1.0 CB A:ILE43 4.3 23.0 1.0 C A:GLN102 4.3 18.5 1.0 CB A:GLN102 4.3 17.0 1.0 CA A:THR103 4.3 19.5 1.0 CD A:ARG214 4.4 20.3 1.0 C A:ALA45 4.6 19.6 1.0 CD1 A:ILE43 4.7 26.0 1.0 O A:ARG42 4.7 24.2 1.0 N A:ALA45 4.7 19.3 1.0 CA A:ARG44 4.8 21.1 1.0 O A:GLY101 4.9 18.7 1.0 N A:ILE43 4.9 23.8 1.0

Y.Moriwaki, M.Yato, T.Terada, S.Saito, N.Nukui, T.Iwasaki, T.Nishi, Y.Kawaguchi, K.Okamoto, T.Arakawa, C.Yamada, S.Fushinobu, K.Shimizu. Understanding the Molecular Mechanism Underlying the High Catalytic Activity Ofp-Hydroxybenzoate Hydroxylase Mutants For Producing Gallic Acid. Biochemistry V. 58 4543 2019.
ISSN: ISSN 0006-2960
PubMed: 31639299
DOI: 10.1021/ACS.BIOCHEM.9B00443