Bromine in PDB 3hzw: Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb)

The structure of Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb), PDB code: 3hzw was solved by C.A.H.Fernandes, D.P.Marchi-Salvador, 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)	50.77 / 2.28
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.670, 62.460, 87.077, 90.00, 90.00, 90.00
R / Rfree (%)	23.5 / 25.4

The binding sites of Bromine atom in the Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) (pdb code 3hzw). 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 Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb), PDB code: 3hzw:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb)


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) within 5.0Å range: probe atom residue distance (Å) B Occ A:Br201 b:71.0 occ:0.38 BR A:PBP201 0.0 71.0 0.4 CZ A:PBP201 1.9 66.3 0.4 CE2 A:PBP201 2.9 66.3 0.7 CE1 A:PBP201 2.9 65.7 0.5 CA A:GLY30 3.8 58.9 1.0 C A:GLY30 3.9 61.4 0.9 CG1 B:VAL31 4.0 58.0 0.8 O A:GLY23 4.0 39.5 1.0 CD2 A:PBP201 4.2 63.4 1.0 CD1 A:PBP201 4.2 63.4 1.0 O A:GLY30 4.2 61.5 1.0 CA A:GLY23 4.4 39.9 1.0 N A:VAL31 4.4 64.0 0.8 N A:GLY30 4.6 54.5 1.0 C A:GLY23 4.7 40.4 0.8 CG A:PBP201 4.7 61.7 0.7 CD2 A:LEU2 4.8 43.7 1.0

Bromine binding site 2 out of 2 in the Crystal Structure of Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb)


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 Bothropstoxin-I Chemically Modified By P- Bromophenacyl Bromide (Bpb) within 5.0Å range: probe atom residue distance (Å) B Occ B:Br201 b:70.2 occ:0.40 BR B:PBP201 0.0 70.2 0.4 CZ B:PBP201 1.9 65.7 1.0 CE2 B:PBP201 2.9 64.9 0.6 CE1 B:PBP201 2.9 65.2 1.0 O B:HOH335 3.0 52.0 1.0 CA B:GLY30 3.7 50.2 1.0 O B:GLY23 3.9 40.2 0.8 CA B:GLY23 4.1 39.9 1.0 CD2 B:PBP201 4.2 62.1 1.0 C B:GLY30 4.2 52.9 1.0 O A:HOH353 4.2 56.1 1.0 CD1 B:PBP201 4.2 62.3 1.0 CG2 A:VAL31 4.3 67.3 0.7 N B:GLY30 4.4 47.7 1.0 C B:GLY23 4.5 40.7 0.9 N B:VAL31 4.6 56.6 1.0 O B:GLY30 4.7 52.0 1.0 CG B:PBP201 4.7 59.9 0.4 O B:TYR22 4.8 37.8 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