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Bromine in PDB 2ag6: Crystal Structure of P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine

Enzymatic activity of Crystal Structure of P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine

All present enzymatic activity of Crystal Structure of P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine:
6.1.1.1;

Protein crystallography data

The structure of Crystal Structure of P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine, PDB code: 2ag6 was solved by J.M.Turner, J.Graziano, G.Spraggon, P.G.Schultz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.55 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 102.719, 102.719, 70.598, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 24.7

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine (pdb code 2ag6). 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 P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine, PDB code: 2ag6:

Bromine binding site 1 out of 1 in 2ag6

Go back to Bromine Binding Sites List in 2ag6
Bromine binding site 1 out of 1 in the Crystal Structure of P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine


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 P-Bromo-L-Phenylalanine-Trna Sythetase in Complex with P-Bromo-L-Phenylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br315

b:51.3
occ:1.00
 BR A:4BF315 0.0 51.3 1.0
CZ A:4BF315 1.8 32.0 1.0
CE2 A:4BF315 2.8 29.4 1.0
CE1 A:4BF315 2.8 29.0 1.0
CG A:HIS160 3.5 42.6 1.0
OH A:TYR161 3.5 47.4 1.0
ND1 A:HIS160 3.5 44.5 1.0
CD2 A:LEU65 3.7 41.9 1.0
O A:GLN155 3.7 40.6 1.0
CD2 A:HIS160 3.8 36.6 1.0
CE1 A:HIS160 3.9 37.7 1.0
CB A:HIS160 3.9 41.8 1.0
CG A:GLN155 4.0 39.4 1.0
CD1 A:4BF315 4.0 30.8 1.0
NE2 A:HIS160 4.0 43.2 1.0
CD2 A:4BF315 4.0 30.5 1.0
O A:HOH333 4.1 34.6 1.0
CZ A:TYR161 4.2 40.2 1.0
CA A:GLN155 4.2 38.4 1.0
C A:GLN155 4.4 39.0 1.0
CD2 A:LEU32 4.4 43.4 1.0
CG A:4BF315 4.5 31.6 1.0
CB A:GLN155 4.5 35.7 1.0
CE2 A:TYR161 4.7 43.1 1.0
CE1 A:TYR161 4.7 41.0 1.0
CD A:GLN155 4.8 37.2 1.0
CE1 A:HIS70 5.0 39.8 1.0

Reference:

J.M.Turner, J.Graziano, G.Spraggon, P.G.Schultz. Structural Plasticity of An Aminoacyl-Trna Synthetase Active Site Proc.Natl.Acad.Sci.Usa V. 103 6483 2006.
ISSN: ISSN 0027-8424
PubMed: 16618920
DOI: 10.1073/PNAS.0601756103
Page generated: Mon Jul 7 04:03:36 2025

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