Bromine in PDB 1eba: Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby)

The structure of Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby), PDB code: 1eba was solved by O.Livnah, E.A.Stura, I.A.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.70
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.890, 75.009, 130.527, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 29.9

The binding sites of Bromine atom in the Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby) (pdb code 1eba). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby), PDB code: 1eba:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br4 b:61.8 occ:1.00 BR1 C:DBY4 0.0 61.8 1.0 CE1 C:DBY4 1.8 55.0 1.0 CZ C:DBY4 2.8 55.4 1.0 CD1 C:DBY4 2.8 56.4 1.0 OH C:DBY4 2.9 52.2 1.0 CE2 D:PHE8 3.4 36.3 1.0 CZ D:PHE8 3.6 38.5 1.0 CD2 D:PHE8 3.7 36.8 1.0 CE1 D:PHE8 4.0 33.7 1.0 CE2 C:DBY4 4.1 57.1 1.0 CG D:PHE8 4.1 38.8 1.0 CG C:DBY4 4.1 53.7 1.0 CD1 D:PHE8 4.2 36.1 1.0 CG2 C:THR3 4.6 43.9 1.0 CD2 C:DBY4 4.6 57.5 1.0 N D:PHE8 4.7 45.6 1.0 CB C:THR3 5.0 43.4 1.0 CZ3 D:TRP13 5.0 40.8 1.0 CB D:PHE8 5.0 41.5 1.0

Bromine binding site 2 out of 4 in the Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby) within 5.0Å range: probe atom residue distance (Å) B Occ C:Br4 b:70.0 occ:1.00 BR2 C:DBY4 0.0 70.0 1.0 CE2 C:DBY4 1.8 57.1 1.0 CZ C:DBY4 2.8 55.4 1.0 CD2 C:DBY4 2.8 57.5 1.0 OH C:DBY4 3.0 52.2 1.0 CG C:PRO17 3.0 49.1 1.0 N B:SER92 3.5 34.5 1.0 CD2 B:PHE93 3.8 21.0 1.0 N B:PHE93 3.8 31.1 1.0 CD C:PRO17 3.8 50.8 1.0 CB B:SER91 3.9 30.2 1.0 CB C:PRO17 4.0 50.0 1.0 C B:SER91 4.0 31.9 1.0 CE1 C:DBY4 4.1 55.0 1.0 CG C:DBY4 4.1 53.7 1.0 CA B:SER91 4.1 30.2 1.0 CA B:SER92 4.2 36.1 1.0 N C:PRO17 4.2 52.1 1.0 CA C:PRO17 4.3 54.1 1.0 C B:SER92 4.4 37.7 1.0 O C:CYS15 4.4 40.8 1.0 CB B:SER92 4.4 34.5 1.0 CE2 B:PHE93 4.5 22.4 1.0 OG B:SER91 4.5 35.4 1.0 CD1 C:DBY4 4.6 56.4 1.0 CB B:PHE93 4.6 25.1 1.0 CG B:PHE93 4.6 21.2 1.0 CA B:PHE93 4.7 26.9 1.0 C C:LYS16 4.7 49.7 1.0 O B:SER91 4.8 31.4 1.0 N B:VAL94 4.9 28.3 1.0 CG2 B:VAL94 5.0 28.3 1.0

Bromine binding site 3 out of 4 in the Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby) within 5.0Å range: probe atom residue distance (Å) B Occ D:Br4 b:51.4 occ:1.00 BR1 D:DBY4 0.0 51.4 1.0 CE1 D:DBY4 1.8 44.4 1.0 CD1 D:DBY4 2.8 45.2 1.0 CZ D:DBY4 2.8 45.4 1.0 OH D:DBY4 3.0 41.3 1.0 CE2 D:DBY4 4.1 46.6 1.0 CG D:DBY4 4.1 44.5 1.0 CZ C:PHE8 4.1 22.6 1.0 CE2 C:PHE8 4.2 18.7 1.0 CE1 C:PHE8 4.3 26.8 1.0 CE2 A:PHE93 4.4 27.9 1.0 CD2 A:PHE93 4.5 30.0 1.0 CD2 C:PHE8 4.5 25.1 1.0 CB A:SER92 4.5 25.6 1.0 CD2 D:DBY4 4.6 48.3 1.0 CD1 C:PHE8 4.7 20.9 1.0 N D:THR3 4.7 35.9 1.0 CG C:PHE8 4.7 24.8 1.0 N A:SER92 4.8 31.4 1.0 CZ3 C:TRP13 4.9 36.4 1.0 OG A:SER92 5.0 35.2 1.0 CA D:THR3 5.0 38.5 1.0

Bromine binding site 4 out of 4 in the Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Complex Between the Extracellular Domain of Erythropoietin (Epo) Receptor [Ebp] and An Inactive Peptide [EMP33] Contains 3,5-Dibromotyrosine in Position 4 (Denoted Dby) within 5.0Å range: probe atom residue distance (Å) B Occ D:Br4 b:48.3 occ:1.00 BR2 D:DBY4 0.0 48.3 1.0 CE2 D:DBY4 1.8 46.6 1.0 CD2 D:DBY4 2.8 48.3 1.0 CZ D:DBY4 2.8 45.4 1.0 OH D:DBY4 3.0 41.3 1.0 CB D:PRO17 3.3 54.1 1.0 CA D:PRO17 3.6 56.3 1.0 CG1 A:VAL94 3.8 33.1 1.0 CB A:PHE93 3.9 29.0 1.0 CE1 D:DBY4 4.1 44.4 1.0 CG D:DBY4 4.1 44.5 1.0 N A:PHE93 4.3 27.3 1.0 CA A:PHE93 4.4 26.6 1.0 CD2 A:PHE93 4.5 30.0 1.0 N D:PRO17 4.6 55.7 1.0 CG D:PRO17 4.6 50.5 1.0 N A:VAL94 4.6 30.3 1.0 CD1 D:DBY4 4.6 45.2 1.0 C A:PHE93 4.6 28.5 1.0 C D:PRO17 4.7 57.5 1.0 CG A:PHE93 4.7 30.0 1.0 CD D:PRO17 4.9 54.0 1.0 N D:GLN18 5.0 57.2 1.0

O.Livnah, D.L.Johnson, E.A.Stura, F.X.Farrell, F.P.Barbone, Y.You, K.D.Liu, M.A.Goldsmith, W.He, C.D.Krause, S.Pestka, L.K.Jolliffe, I.A.Wilson. An Antagonist Peptide-Epo Receptor Complex Suggests That Receptor Dimerization Is Not Sufficient For Activation. Nat.Struct.Biol. V. 5 993 1998.
ISSN: ISSN 1072-8368
PubMed: 9808045
DOI: 10.1038/2965