Bromine in PDB 2fkk: Crystal Structure of the C-Terminal Domain of the Bacteriophage T4 Gene Product 10

The structure of Crystal Structure of the C-Terminal Domain of the Bacteriophage T4 Gene Product 10, PDB code: 2fkk was solved by P.G.Leiman, M.M.Shneider, V.V.Mesyanzhinov, M.G.Rossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.20
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.843, 69.843, 119.672, 90.00, 90.00, 120.00
R / Rfree (%)	12 / 13.6

The binding sites of Bromine atom in the Crystal Structure of the C-Terminal Domain of the Bacteriophage T4 Gene Product 10 (pdb code 2fkk). 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 the Bacteriophage T4 Gene Product 10, PDB code: 2fkk:

Bromine binding site 1 out of 1 in the Crystal Structure of the C-Terminal Domain of the Bacteriophage T4 Gene Product 10


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 the Bacteriophage T4 Gene Product 10 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br701 b:15.5 occ:0.33 O A:HOH1049 2.7 18.0 0.3 O A:ASN588 2.8 12.9 1.0 OD1 A:ASN588 2.9 12.8 1.0 C A:ASN588 3.6 12.0 1.0 CG A:ASN588 3.6 12.5 1.0 N A:TRS801 3.7 12.4 0.3 HA A:ASN588 3.8 14.7 1.0 HB3 A:GLN590 4.0 14.7 1.0 CA A:ASN588 4.1 12.3 1.0 HD21 A:ASN588 4.2 15.8 1.0 ND2 A:ASN588 4.2 13.1 1.0 H A:GLN590 4.3 14.2 1.0 N A:ILE589 4.4 12.1 1.0 HA A:ILE589 4.4 14.3 1.0 CB A:ASN588 4.5 12.5 1.0 N A:GLN590 4.6 11.8 1.0 CA A:ILE589 4.8 11.9 1.0 C A:ILE589 4.8 11.7 1.0 HD22 A:ASN588 4.9 15.8 1.0 HB3 A:ASN588 4.9 15.0 1.0 CB A:GLN590 4.9 12.3 1.0

P.G.Leiman, M.M.Shneider, V.V.Mesyanzhinov, M.G.Rossmann. Evolution of Bacteriophage Tails: Structure of T4 Gene Product 10 J.Mol.Biol. V. 358 912 2006.
ISSN: ISSN 0022-2836
PubMed: 16554069
DOI: 10.1016/J.JMB.2006.02.058