Crystal Structure and Thermodynamic Characterization of the EphB4 Receptor in Complex with an ephrin-B2 Antagonist Peptide Reveals the Determinants for Receptor Specificity. Determined by X-ray diffraction at 1.65 Å resolution. Released 18 Jul 2006.
Explore 2BBA in 3D Show helices and sheets RCSB PDB PDBe
2BBA contains 4 α-helices and 18 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17-22 | 6 | 1 |
| α-helix | 23-25 | 3 | |
| β-strand | 33-35 | 3 | 2 |
| β-strand | 43-48 | 6 | 1 |
| β-strand | 54-61 | 8 | 1 |
| β-strand | 70-74 | 5 | 2 |
| α-helix | 75-77 | 3 | |
| β-strand | 78-79 | 2 | 2 |
| β-strand | 86-94 | 9 | 1 |
| β-strand | 95 | 1 | 3 |
| α-helix | 97-99 | 3 | |
| β-strand | 110-118 | 9 | 2 |
| β-strand | 132 | 1 | 4 |
| β-strand | 135 | 1 | 4 |
| β-strand | 136-142 | 7 | 2 |
| β-strand | 147 | 1 | 3 |
| β-strand | 148 | 1 | 5 |
| β-strand | 156 | 1 | 5 |
| β-strand | 160-166 | 7 | 1 |
| β-strand | 173-181 | 9 | 2 |
| β-strand | 184-195 | 12 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 261-263 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-B receptor 4 | A | protein | 185 | Homo sapiens | P54760 (AlphaFold model) |
| Agonist peptide | P | protein | 15 |
>2BBA_1 Ephrin type-B receptor 4 (chains A) HHHHHEETLLNTKLETADLKWVTFPQVDGQWEELSGLDEEQHSVRTYEVCDVQRAPGQAH WLRTGWVPRRGAVHVYATLRFTMLECLSLPRAGRSCKETFTVFYYESDADTATALTPAWM ENPYIKVDTVAAEHLTRKRPGAEATGKVNVKTLRLGPLSKAGFYLAFQDQGACMALLSLH LFYKK
>2BBA_2 Agonist peptide (chains P) TNYLFSPNGPIARAW
Structure and thermodynamic characterization of the EphB4/Ephrin-B2 antagonist peptide complex reveals the determinants for receptor specificity. Chrencik, J.E., Brooun, A., Recht, M.I. et al. Structure (2006) 14:321-330. DOI 10.1016/j.str.2005.11.011 · PubMed
Other PDB entries of the same protein (UniProt P54760 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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