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Bromine in PDB 3lwo: Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU

Protein crystallography data

The structure of Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU, PDB code: 3lwo was solved by J.Zhou, B.Liang, C.Lv, W.Yang, H.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.67 / 2.85
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 184.523, 62.698, 85.335, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 24

Other elements in 3lwo:

The structure of Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU (pdb code 3lwo). 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 Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU, PDB code: 3lwo:

Bromine binding site 1 out of 1 in 3lwo

Go back to Bromine Binding Sites List in 3lwo
Bromine binding site 1 out of 1 in the Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of H/Aca Rnp Bound to A Substrate Rna Containing 5BRU within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Br10

b:0.4
occ:1.00
BR E:5BU10 0.0 0.4 1.0
C5 E:5BU10 1.9 84.0 1.0
C6 E:5BU10 2.8 86.6 1.0
C4 E:5BU10 2.9 78.3 1.0
O4 E:5BU10 3.2 81.8 1.0
CG1 A:ILE183 3.6 58.4 1.0
O A:THR181 3.6 87.1 1.0
N A:ILE183 3.8 66.1 1.0
CD2 A:LEU203 3.9 61.2 1.0
CZ A:TYR113 4.0 58.8 1.0
OH A:TYR113 4.0 72.1 1.0
CB A:ILE183 4.0 59.2 1.0
N1 E:5BU10 4.1 84.1 1.0
N3 E:5BU10 4.1 85.9 1.0
CE2 A:TYR113 4.1 48.1 1.0
CE1 A:TYR113 4.5 59.9 1.0
CA A:TYR182 4.5 62.7 1.0
CA A:ILE183 4.5 66.8 1.0
C A:TYR182 4.7 72.8 1.0
C2 E:5BU10 4.7 91.1 1.0
C A:THR181 4.7 75.8 1.0
CD2 A:TYR113 4.8 54.2 1.0
CD1 A:ILE183 4.8 56.6 1.0

Reference:

J.Zhou, C.Lv, B.Liang, M.Chen, W.Yang, H.Li. Glycosidic Bond Conformation Preference Plays A Pivotal Role in Catalysis of Rna Pseudouridylation: A Combined Simulation and Structural Study. J.Mol.Biol. V. 401 690 2010.
ISSN: ISSN 0022-2836
PubMed: 20615421
DOI: 10.1016/J.JMB.2010.06.061
Page generated: Sat Dec 12 02:13:24 2020

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