Atomistry » Bromine » PDB 1iha-1m9r » 1lnt
Atomistry »
  Bromine »
    PDB 1iha-1m9r »
      1lnt »

Bromine in PDB 1lnt: Crystal Structure of the Highly Conserved Rna Internal Loop of Srp

Protein crystallography data

The structure of Crystal Structure of the Highly Conserved Rna Internal Loop of Srp, PDB code: 1lnt was solved by J.Deng, Y.Xiong, B.Pan, M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 35.610, 35.610, 133.960, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 22.5

Other elements in 1lnt:

The structure of Crystal Structure of the Highly Conserved Rna Internal Loop of Srp also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Calcium (Ca) 3 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp (pdb code 1lnt). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp, PDB code: 1lnt:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in 1lnt

Go back to Bromine Binding Sites List in 1lnt
Bromine binding site 1 out of 2 in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp


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 Highly Conserved Rna Internal Loop of Srp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br11

b:26.1
occ:1.00
BR A:CBV11 0.0 26.1 1.0
C5 A:CBV11 1.9 22.4 1.0
C6 A:CBV11 2.8 20.3 1.0
C4 A:CBV11 2.9 21.8 1.0
O A:HOH310 3.1 46.5 1.0
N4 A:CBV11 3.2 21.5 1.0
O A:HOH309 3.6 32.2 1.0
C5 A:C10 3.6 22.9 1.0
C6 A:C10 3.7 20.6 1.0
O A:HOH220 3.7 30.4 1.0
C4 A:C10 3.7 23.8 1.0
O1P A:CBV11 3.7 24.8 1.0
N1 A:C10 3.8 20.7 1.0
N3 A:C10 3.9 22.0 1.0
C2 A:C10 3.9 21.1 1.0
N1 A:CBV11 4.1 19.5 1.0
N3 A:CBV11 4.1 20.9 1.0
C3' A:C10 4.2 22.2 1.0
C2' A:C10 4.3 21.9 1.0
N4 A:C10 4.3 22.3 1.0
O A:HOH243 4.3 35.4 1.0
O5' A:CBV11 4.4 22.1 1.0
P A:CBV11 4.6 23.1 1.0
C2 A:CBV11 4.6 21.4 1.0
MG A:MG104 4.6 42.0 1.0
C1' A:C10 4.6 21.9 1.0
O2 A:C10 4.6 21.1 1.0
O5' A:C10 4.9 23.9 1.0
O A:HOH234 4.9 34.5 1.0
O3' A:C10 4.9 21.8 1.0

Bromine binding site 2 out of 2 in 1lnt

Go back to Bromine Binding Sites List in 1lnt
Bromine binding site 2 out of 2 in the Crystal Structure of the Highly Conserved Rna Internal Loop of Srp


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of the Highly Conserved Rna Internal Loop of Srp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br22

b:26.6
occ:1.00
BR B:CBV22 0.0 26.6 1.0
C5 B:CBV22 1.9 20.5 1.0
C6 B:CBV22 2.9 21.3 1.0
C4 B:CBV22 2.9 20.9 1.0
N4 B:CBV22 3.1 17.6 1.0
O B:HOH224 3.3 35.4 1.0
O1P B:CBV22 3.6 23.9 1.0
C8 B:G21 3.7 22.7 1.0
O B:HOH207 3.7 27.8 1.0
N7 B:G21 3.7 22.6 1.0
O B:HOH205 3.7 20.6 1.0
O B:HOH238 3.8 36.1 1.0
C3' B:G21 4.1 22.4 1.0
O B:HOH221 4.1 28.8 1.0
N1 B:CBV22 4.1 20.5 1.0
N9 B:G21 4.1 21.4 1.0
N3 B:CBV22 4.1 20.7 1.0
C5 B:G21 4.2 20.9 1.0
O5' B:G21 4.2 27.7 1.0
OP2 B:G21 4.4 27.1 1.0
O5' B:CBV22 4.4 22.1 1.0
C4 B:G21 4.5 19.7 1.0
P B:CBV22 4.5 23.2 1.0
C2' B:G21 4.6 20.9 1.0
C2 B:CBV22 4.7 19.6 1.0
O B:HOH218 4.8 29.6 1.0
O3' B:G21 4.8 23.0 1.0
C1' B:G21 4.9 19.9 1.0
C6 B:G21 5.0 21.2 1.0
C4' B:G21 5.0 27.2 1.0
P B:G21 5.0 28.7 1.0

Reference:

J.Deng, Y.Xiong, B.Pan, M.Sundaralingam. Structure of An Rna Dodecamer Containing A Fragment From Srp Domain IV of Escherichia Coli. Acta Crystallogr.,Sect.D V. 59 1004 2003.
ISSN: ISSN 0907-4449
PubMed: 12777762
DOI: 10.1107/S0907444903006747
Page generated: Wed Jul 10 16:51:17 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy