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Bromine in PDB 4tqf: Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp

Enzymatic activity of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp

All present enzymatic activity of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp:
6.1.1.26;

Protein crystallography data

The structure of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp, PDB code: 4tqf was solved by A.Nakamura, P.O'donoghue, D.Soll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.20 / 2.71
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 105.110, 105.110, 70.290, 90.00, 90.00, 120.00
R / Rfree (%) 16.8 / 21.1

Other elements in 4tqf:

The structure of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp (pdb code 4tqf). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp, PDB code: 4tqf:

Bromine binding site 1 out of 1 in 4tqf

Go back to Bromine Binding Sites List in 4tqf
Bromine binding site 1 out of 1 in the Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of the C-Terminal Domain of Ifrs Bound with 2-(5- Bromothienyl)-L-Ala and Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br504

b:0.4
occ:1.00
BR A:33W504 0.0 0.4 1.0
C3 A:33W504 1.9 0.6 1.0
C4 A:33W504 2.9 0.7 1.0
S2 A:33W504 3.1 0.1 1.0
CD1 A:ILE348 3.5 77.0 1.0
C5 A:33W504 4.1 0.2 1.0
CB A:ALA302 4.2 58.9 1.0
CE2 A:TYR306 4.2 64.7 1.0
CZ A:TYR306 4.2 63.0 1.0
O A:ALA302 4.2 51.7 1.0
CD2 A:TYR306 4.2 55.7 1.0
CE1 A:TYR306 4.3 60.9 1.0
CA A:ALA302 4.3 53.2 1.0
C1 A:33W504 4.3 94.4 1.0
CG A:TYR306 4.3 54.6 1.0
CD1 A:TYR306 4.4 56.6 1.0
CG1 A:ILE348 4.4 72.4 1.0
C A:ALA302 4.7 49.9 1.0
CZ3 A:TRP417 4.7 63.8 1.0
OH A:TYR306 4.7 53.9 1.0
CH2 A:TRP417 4.8 61.2 1.0
N A:TYR306 4.8 58.0 1.0
CB A:LEU305 4.9 40.8 1.0
CD1 A:LEU309 4.9 50.8 1.0

Reference:

L.T.Guo, Y.S.Wang, A.Nakamura, D.Eiler, J.Kavran, M.Wong, L.Kiessling, T.Steitz, P.O'donoghue, D.Soll. Polyspecific Pyrrolysyl-Trna Synthetases From Directed Evolution Proc.Natl.Acad.Sci.Usa 2014.
ISSN: ESSN 1091-6490
Page generated: Wed Jul 10 22:37:57 2024

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