Bromine in PDB 3i03: Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) - Monomeric Form at A High Resolution

The structure of Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) - Monomeric Form at A High Resolution, PDB code: 3i03 was solved by D.P.Marchi-Salvador, C.A.H.Fernandes, A.M.Soares, M.R.M.Fontes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.98 / 1.48
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	56.846, 78.294, 66.615, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 22.3

The binding sites of Bromine atom in the Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) - Monomeric Form at A High Resolution (pdb code 3i03). 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 Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) - Monomeric Form at A High Resolution, PDB code: 3i03:

Bromine binding site 1 out of 1 in the Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) - Monomeric Form at A High Resolution


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 Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) - Monomeric Form at A High Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Br201 b:35.4 occ:0.69 BR A:PBP201 0.0 35.4 0.7 CZ A:PBP201 1.5 31.7 0.4 CE1 A:PBP201 2.5 32.3 1.0 CE2 A:PBP201 2.5 31.9 1.0 CA A:GLY29 2.7 20.9 0.7 O A:HOH618 3.0 89.3 1.0 O A:HOH325 3.0 23.5 1.0 C A:GLY29 3.4 21.5 1.0 N A:GLY29 3.4 19.2 1.0 O A:GLY22 3.5 17.4 1.0 CA A:GLY22 3.7 16.5 1.0 CD1 A:PBP201 3.8 31.6 1.0 CD2 A:PBP201 3.8 31.2 0.8 O2 A:IPA211 3.8 40.5 1.0 O A:GLY29 3.9 21.1 1.0 C A:GLY22 3.9 16.6 1.0 C1 A:IPA211 4.0 40.6 1.0 C2 A:IPA211 4.1 40.7 1.0 O A:TYR21 4.1 17.7 1.0 N A:VAL30 4.1 22.7 1.0 CG A:PBP201 4.3 30.2 1.0 O A:HOH411 4.4 28.4 1.0 C A:CYS28 4.5 19.4 1.0 O A:HOH479 4.6 55.3 0.6 N A:GLY22 4.7 16.5 1.0 C A:TYR21 4.7 17.0 1.0 O A:CYS28 4.9 21.3 0.9 O A:HOH329 5.0 25.2 1.0

C.A.Fernandes, D.P.Marchi-Salvador, G.M.Salvador, M.C.Silva, T.R.Costa, A.M.Soares, M.R.Fontes. Comparison Between Apo and Complexed Structures of Bothropstoxin-I Reveals the Role of LYS122 and Ca(2+)-Binding Loop Region For the Catalytically Inactive LYS49-Pla(2)S. J.Struct.Biol. V. 171 31 2010.
ISSN: ISSN 1047-8477
PubMed: 20371382
DOI: 10.1016/J.JSB.2010.03.019