Atomistry » Bromine » PDB 1p2x-1to3 » 1t0s
Atomistry »
  Bromine »
    PDB 1p2x-1to3 »
      1t0s »

Bromine in PDB 1t0s: Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound

Protein crystallography data

The structure of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound, PDB code: 1t0s was solved by M.H.Sazinsky, J.Bard, A.Di Donato, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.47 / 2.20
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.242, 183.242, 67.671, 90.00, 90.00, 120.00
R / Rfree (%) 23.6 / 27.3

Other elements in 1t0s:

The structure of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound (pdb code 1t0s). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 6 binding sites of Bromine where determined in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound, PDB code: 1t0s:
Jump to Bromine binding site number: 1; 2; 3; 4; 5; 6;

Bromine binding site 1 out of 6 in 1t0s

Go back to Bromine Binding Sites List in 1t0s
Bromine binding site 1 out of 6 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound


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 Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br503

b:87.4
occ:1.00
BR4 A:BML503 0.0 87.4 1.0
C4 A:BML503 1.9 80.6 1.0
C3 A:BML503 2.8 80.2 1.0
C5 A:BML503 2.9 79.5 1.0
CD1 A:PHE269 3.9 52.8 1.0
C6 A:BML503 4.1 77.7 1.0
CD1 A:LEU272 4.1 58.3 1.0
CZ A:PHE196 4.2 46.4 1.0
C2 A:BML503 4.2 78.3 1.0
NE2 A:GLN204 4.2 71.1 1.0
CE1 A:PHE269 4.3 52.9 1.0
CD2 A:LEU268 4.4 52.0 1.0
CE1 A:PHE196 4.4 46.0 1.0
CG A:LEU268 4.5 52.1 1.0
OE1 A:GLN204 4.6 70.2 1.0
CB A:LEU272 4.7 57.1 1.0
CA A:PHE269 4.7 53.1 1.0
C1 A:BML503 4.7 77.4 1.0
OG1 A:THR273 4.8 57.4 1.0
O A:LEU268 4.8 50.6 1.0
CD A:GLN204 4.9 69.3 1.0
CG A:PHE269 5.0 54.3 1.0

Bromine binding site 2 out of 6 in 1t0s

Go back to Bromine Binding Sites List in 1t0s
Bromine binding site 2 out of 6 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound


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 Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br504

b:81.4
occ:1.00
BR4 A:BML504 0.0 81.4 1.0
C4 A:BML504 1.8 75.7 1.0
C3 A:BML504 2.8 74.6 1.0
C5 A:BML504 2.9 74.6 1.0
CG2 A:THR273 3.8 56.9 1.0
O1 A:BML503 3.9 75.3 1.0
NE2 A:GLN204 4.0 71.1 1.0
C2 A:BML503 4.1 78.3 1.0
C6 A:BML504 4.1 72.9 1.0
OG1 A:THR273 4.2 57.4 1.0
C2 A:BML504 4.2 72.8 1.0
C1 A:BML503 4.3 77.4 1.0
CG A:GLN204 4.3 66.1 1.0
CD1 A:LEU208 4.4 52.2 1.0
CB A:THR273 4.4 57.2 1.0
CB A:LEU208 4.4 50.0 1.0
CA A:THR273 4.5 56.5 1.0
CD A:GLN204 4.6 69.3 1.0
CG2 A:ILE276 4.6 60.1 1.0
CD2 A:LEU208 4.6 51.4 1.0
C1 A:BML504 4.7 72.9 1.0
CG A:LEU208 4.7 51.5 1.0
CB A:ILE276 4.7 61.7 1.0
CG1 A:ILE276 4.8 62.0 1.0
O A:LEU272 4.8 59.1 1.0

Bromine binding site 3 out of 6 in 1t0s

Go back to Bromine Binding Sites List in 1t0s
Bromine binding site 3 out of 6 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br505

b:74.6
occ:1.00
BR4 A:BML505 0.0 74.6 1.0
C4 A:BML505 1.9 70.9 1.0
C3 A:BML505 2.8 70.6 1.0
C5 A:BML505 2.9 70.4 1.0
CG2 A:THR281 3.4 71.5 1.0
OD2 A:ASP211 3.7 62.2 1.0
CB A:ASP211 3.7 57.4 1.0
CG2 A:ILE276 3.8 60.1 1.0
CZ3 A:TRP89 4.0 48.5 1.0
C5 A:BML504 4.0 74.6 1.0
C6 A:BML504 4.1 72.9 1.0
C6 A:BML505 4.1 70.0 1.0
CG A:ASP211 4.2 59.7 1.0
C2 A:BML505 4.2 70.0 1.0
CE3 A:TRP89 4.4 48.9 1.0
CG2 A:THR92 4.7 44.8 1.0
C1 A:BML505 4.7 70.0 1.0
CB A:THR281 4.7 71.1 1.0
O A:ILE276 4.9 63.1 1.0
OG1 A:THR92 4.9 45.4 1.0
CD1 A:LEU208 5.0 52.2 1.0
CA A:ASP211 5.0 55.5 1.0

Bromine binding site 4 out of 6 in 1t0s

Go back to Bromine Binding Sites List in 1t0s
Bromine binding site 4 out of 6 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br506

b:79.7
occ:1.00
BR4 A:BML506 0.0 79.7 1.0
C4 A:BML506 1.9 75.5 1.0
C3 A:BML506 2.8 74.3 1.0
C5 A:BML506 2.9 74.2 1.0
CD2 A:LEU393 3.5 53.7 1.0
O A:THR392 4.0 51.1 1.0
NE1 A:TRP338 4.1 58.7 1.0
C6 A:BML506 4.1 73.0 1.0
CD1 A:TRP338 4.2 58.7 1.0
C2 A:BML506 4.2 73.3 1.0
CG A:LEU393 4.3 54.4 1.0
C A:THR392 4.5 52.5 1.0
CG2 A:THR341 4.5 50.0 1.0
CA A:LEU393 4.6 54.6 1.0
N A:LEU393 4.7 52.6 1.0
O A:HOH603 4.7 30.8 1.0
C1 A:BML506 4.7 73.3 1.0
CB A:LEU393 5.0 53.6 1.0

Bromine binding site 5 out of 6 in 1t0s

Go back to Bromine Binding Sites List in 1t0s
Bromine binding site 5 out of 6 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 5 of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br331

b:45.0
occ:1.00
BR4 B:BML331 0.0 45.0 1.0
C4 B:BML331 1.9 35.2 1.0
C3 B:BML331 2.8 33.9 1.0
C5 B:BML331 2.9 33.6 1.0
OH B:TYR171 3.7 35.5 1.0
CZ B:TYR171 3.8 37.4 1.0
CD1 B:PHE101 3.8 40.7 1.0
SD A:MET3 3.8 22.9 1.0
CG A:MET3 3.9 31.9 1.0
CB B:PHE101 4.0 33.0 1.0
CE2 B:TYR171 4.1 36.9 1.0
CG B:GLN98 4.1 37.9 1.0
C6 B:BML331 4.1 31.2 1.0
CA B:GLN98 4.2 32.7 1.0
CE1 B:TYR171 4.2 36.6 1.0
C2 B:BML331 4.2 31.2 1.0
CG B:PHE101 4.4 39.5 1.0
O A:HOH607 4.4 52.6 1.0
CB B:GLN98 4.4 33.7 1.0
O B:GLN98 4.6 32.0 1.0
CB A:MET3 4.6 32.9 1.0
C1 B:BML331 4.7 32.7 1.0
CD2 B:TYR171 4.7 34.9 1.0
CE1 B:PHE101 4.8 40.4 1.0
O B:HOH448 4.8 39.1 1.0
CD1 B:TYR171 4.8 33.5 1.0
C B:GLN98 4.9 33.3 1.0
CD B:GLN98 4.9 41.9 1.0

Bromine binding site 6 out of 6 in 1t0s

Go back to Bromine Binding Sites List in 1t0s
Bromine binding site 6 out of 6 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 6 of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase with 4- Bromophenol Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br332

b:66.2
occ:1.00
BR4 B:BML332 0.0 66.2 1.0
C4 B:BML332 1.8 64.1 1.0
C3 B:BML332 2.8 64.8 1.0
C5 B:BML332 2.9 63.5 1.0
O B:GLU231 3.3 32.5 1.0
OE2 B:GLU232 3.5 39.5 1.0
C B:GLU231 3.6 33.2 1.0
CE B:LYS258 3.7 49.3 1.0
CB B:GLU231 3.7 33.0 1.0
CD B:GLU232 3.9 39.4 1.0
NH2 B:ARG265 4.0 37.7 1.0
CG B:LYS258 4.0 41.1 1.0
CB B:GLN236 4.0 40.8 1.0
N B:GLU232 4.0 33.7 1.0
OE1 B:GLU232 4.1 39.6 1.0
C6 B:BML332 4.1 63.9 1.0
CB B:LEU235 4.1 36.3 1.0
N B:GLN236 4.2 38.8 1.0
C2 B:BML332 4.2 64.2 1.0
CA B:GLU231 4.2 33.3 1.0
CD B:LYS258 4.2 45.9 1.0
CA B:GLU232 4.3 34.7 1.0
OE1 B:GLN236 4.5 50.9 1.0
CA B:GLN236 4.6 39.5 1.0
NZ B:LYS258 4.7 53.1 1.0
C1 B:BML332 4.7 63.5 1.0
CZ B:ARG265 4.7 40.0 1.0
O B:HOH425 4.8 54.5 1.0
C B:LEU235 4.8 39.0 1.0
CD1 B:LEU235 4.8 34.5 1.0
CG B:GLU231 4.8 37.0 1.0
NH1 B:ARG265 4.8 35.0 1.0
CG B:GLU232 4.9 35.5 1.0
CG B:LEU235 4.9 36.9 1.0

Reference:

M.H.Sazinsky, J.Bard, A.Di Donato, S.J.Lippard. Crystal Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase From Pseudomonas Stutzeri OX1: Insight Into the Substrate Specificity, Substrate Channeling, and Active Site Tuning of Multicomponent Monooxygenases. J.Biol.Chem. V. 279 30600 2004.
ISSN: ISSN 0021-9258
PubMed: 15096510
DOI: 10.1074/JBC.M400710200
Page generated: Sat Dec 12 02:04:10 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy