Atomistry » Bromine » PDB 4p6j-4tm1 » 4pbr
Atomistry »
  Bromine »
    PDB 4p6j-4tm1 »
      4pbr »

Bromine in PDB 4pbr: Crystal Structure of the M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf)

Enzymatic activity of Crystal Structure of the M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf)

All present enzymatic activity of Crystal Structure of the M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf):
6.1.1.1;

Protein crystallography data

The structure of Crystal Structure of the M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf), PDB code: 4pbr was solved by R.B.Cooley, P.A.Karplus, R.A.Mehl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.30 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 101.260, 101.260, 71.550, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 24.3

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf) (pdb code 4pbr). 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 M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf), PDB code: 4pbr:

Bromine binding site 1 out of 1 in 4pbr

Go back to Bromine Binding Sites List in 4pbr
Bromine binding site 1 out of 1 in the Crystal Structure of the M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf)


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 M. Jannaschii G2 Trna Synthetase Variant Bound to 4-(2-Bromoisobutyramido)-Phenylalanine (Bibaf) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br401

b:42.8
occ:0.45
 BR1 A:2L7401 0.0 42.8 0.5
C10 A:2L7401 2.0 56.8 1.0
C09 A:2L7401 2.7 47.5 1.0
C11 A:2L7401 2.8 57.7 1.0
C13 A:2L7401 2.8 59.2 1.0
O A:ILE33 3.3 35.3 1.0
N08 A:2L7401 3.4 41.2 1.0
O14 A:2L7401 3.4 52.6 1.0
N A:ILE33 3.5 33.3 1.0
C A:ILE33 3.6 27.3 1.0
CB A:GLU65 3.8 29.4 1.0
CA A:GLY32 3.8 30.5 1.0
C A:GLY32 3.9 32.6 1.0
O A:ILE63 3.9 35.6 1.0
CA A:ILE33 4.0 37.3 1.0
N A:GLU65 4.1 31.2 1.0
N A:GLY34 4.2 25.9 1.0
OE2 A:GLU65 4.3 33.5 1.0
C07 A:2L7401 4.5 35.9 1.0
CA A:GLU65 4.5 32.8 1.0
CG2 A:ILE63 4.6 41.9 1.0
C A:ILE63 4.6 32.8 1.0
CA A:GLY34 4.7 25.9 1.0
CB A:ILE63 4.7 43.5 1.0
O A:GLY32 4.8 33.2 1.0
C A:ILE64 4.9 26.9 1.0
C15 A:2L7401 4.9 32.2 1.0

Reference:

R.B.Cooley, P.A.Karplus, R.A.Mehl. Gleaning Unexpected Fruits From Hard-Won Synthetases: Probing Principles of Permissivity in Non-Canonical Amino Acid-Trna Synthetases. Chembiochem V. 15 1810 2014.
ISSN: ESSN 1439-7633
PubMed: 25044993
DOI: 10.1002/CBIC.201402180
Page generated: Wed Jul 10 22:16:14 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy