Structure of the EphA4 LBD in complex with peptide. Determined by X-ray diffraction at 2.41 Å resolution. Released 8 Oct 2014.
Explore 4W4Z in 3D Show helices and sheets RCSB PDB PDBe
4W4Z contains 14 α-helices and 68 β-strands across 8 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 | 30-35 | 6 | 1 |
| β-strand | 46-48 | 3 | 2 |
| β-strand | 55-60 | 6 | 1 |
| β-strand | 66-72 | 7 | 1 |
| β-strand | 82-85 | 4 | 2 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-90 | 2 | 2 |
| β-strand | 97-105 | 9 | 1 |
| α-helix | 108-110 | 3 | |
| β-strand | 119 | 1 | 3 |
| β-strand | 121-129 | 9 | 2 |
| α-helix | 139-141 | 3 | |
| β-strand | 143-149 | 7 | 2 |
| β-strand | 154-158 | 5 | 1 |
| β-strand | 163-173 | 11 | 1 |
| β-strand | 180-187 | 8 | 2 |
| β-strand | 190 | 1 | 3 |
| β-strand | 192-202 | 11 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-35 | 6 | 4 |
| α-helix | 36-38 | 3 | |
| α-helix | 45 | 1 | |
| β-strand | 46-48 | 3 | 5 |
| β-strand | 55-60 | 6 | 4 |
| β-strand | 66-72 | 7 | 4 |
| β-strand | 82-85 | 4 | 5 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-90 | 2 | 5 |
| β-strand | 97-106 | 10 | 4 |
| β-strand | 119 | 1 | 6 |
| β-strand | 121-129 | 9 | 5 |
| α-helix | 139-141 | 3 | |
| α-helix | 142 | 1 | |
| β-strand | 143-149 | 7 | 5 |
| β-strand | 154-158 | 5 | 4 |
| β-strand | 163-173 | 11 | 4 |
| β-strand | 180-187 | 8 | 5 |
| β-strand | 190 | 1 | 6 |
| β-strand | 191-202 | 12 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-35 | 6 | 4 |
| α-helix | 36-38 | 3 | |
| β-strand | 46-48 | 3 | 7 |
| β-strand | 55-60 | 6 | 4 |
| β-strand | 66-72 | 7 | 4 |
| β-strand | 82-85 | 4 | 7 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-90 | 2 | 7 |
| β-strand | 97-105 | 9 | 4 |
| β-strand | 119 | 1 | 8 |
| β-strand | 121-129 | 9 | 7 |
| α-helix | 139-141 | 3 | |
| β-strand | 143-149 | 7 | 7 |
| β-strand | 153-158 | 6 | 4 |
| β-strand | 163-173 | 11 | 4 |
| β-strand | 180-187 | 8 | 7 |
| β-strand | 190 | 1 | 8 |
| β-strand | 192-202 | 11 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 30-35 | 6 | 1 |
| α-helix | 36-38 | 3 | |
| β-strand | 46-48 | 3 | 9 |
| β-strand | 55-60 | 6 | 1 |
| β-strand | 66-73 | 8 | 1 |
| β-strand | 82-85 | 4 | 9 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-90 | 2 | 9 |
| β-strand | 97-105 | 9 | 1 |
| α-helix | 108-110 | 3 | |
| β-strand | 119 | 1 | 10 |
| β-strand | 121-129 | 9 | 9 |
| β-strand | 143-149 | 7 | 9 |
| β-strand | 154-158 | 5 | 1 |
| β-strand | 163-173 | 11 | 1 |
| β-strand | 180-187 | 8 | 9 |
| β-strand | 190 | 1 | 10 |
| β-strand | 191-202 | 12 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-6 | 2 | 11 |
| β-strand | 10-11 | 2 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-A receptor 4 | A, B, C, D | protein | 179 | Homo sapiens | P54764 (AlphaFold model) |
| APY-bAla8.am peptide | E, F, G, H | protein | 13 | synthetic construct |
>4W4Z_1 Ephrin type-A receptor 4 (chains A, B, C, D) GPGNEVTLLDSRSVQGELGWIASPLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLR TDWITREGAQRVYIEIKFTLRDCNSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKI DTIAADESFTQVDIGDRIMKLNTEIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKA
>4W4Z_2 APY-bAla8.am peptide (chains E, F, G, H) APYCVYRXSWSCX
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEZ | Hexane-1,6-diol | C6 H14 O2 | 7 |
Water and common crystallization additives (GOL) are not listed.
Development and Structural Analysis of a Nanomolar Cyclic Peptide Antagonist for the EphA4 Receptor. Lamberto, I., Lechtenberg, B.C., Olson, E.J. et al. ACS Chem Biol (2014) 9:2787-2795. DOI 10.1021/cb500677x · PubMed
Other PDB entries of the same protein (UniProt P54764 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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