crystal structure of the human EphA4 ectodomain. Determined by X-ray diffraction at 3.65 Å resolution. Released 3 Jul 2013.
Explore 4BK4 in 3D Show helices and sheets RCSB PDB PDBe
4BK4 contains 28 α-helices and 78 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 |
|---|---|---|---|
| α-helix | 31 | 1 | |
| β-strand | 32-34 | 3 | 1 |
| β-strand | 46-48 | 3 | 2 |
| β-strand | 55 | 1 | 1 |
| β-strand | 59 | 1 | 3 |
| β-strand | 67 | 1 | 3 |
| β-strand | 70-72 | 3 | 1 |
| β-strand | 82-85 | 4 | 2 |
| α-helix | 86-88 | 3 | |
| β-strand | 89-90 | 2 | 2 |
| β-strand | 97-105 | 9 | 1 |
| β-strand | 121-129 | 9 | 2 |
| β-strand | 143-149 | 7 | 2 |
| β-strand | 155-156 | 2 | 4 |
| β-strand | 165-166 | 2 | 4 |
| β-strand | 167-173 | 7 | 1 |
| β-strand | 180-187 | 8 | 2 |
| β-strand | 192-201 | 10 | 1 |
| β-strand | 203-204 | 2 | 5 |
| β-strand | 208-209 | 2 | 6 |
| β-strand | 212-213 | 2 | 6 |
| β-strand | 217-218 | 2 | 5 |
| α-helix | 219-220 | 2 | |
| β-strand | 227-229 | 3 | 7 |
| α-helix | 231-232 | 2 | |
| β-strand | 233 | 1 | 6 |
| α-helix | 234 | 1 | |
| β-strand | 237 | 1 | 8 |
| β-strand | 244 | 1 | 9 |
| β-strand | 245-247 | 3 | 7 |
| β-strand | 253 | 1 | 7 |
| β-strand | 257 | 1 | 9 |
| α-helix | 261 | 1 | |
| β-strand | 262 | 1 | 8 |
| α-helix | 263 | 1 | |
| β-strand | 266-267 | 2 | 10 |
| β-strand | 274-275 | 2 | 10 |
| α-helix | 276-277 | 2 | |
| β-strand | 280-281 | 2 | 11 |
| α-helix | 289-290 | 2 | |
| β-strand | 291-292 | 2 | 11 |
| α-helix | 293-294 | 2 | |
| α-helix | 298-301 | 4 | |
| β-strand | 304 | 1 | 11 |
| α-helix | 308-310 | 3 | |
| β-strand | 314 | 1 | 12 |
| α-helix | 324-325 | 2 | |
| β-strand | 326 | 1 | 12 |
| α-helix | 327-329 | 3 | |
| β-strand | 335-339 | 5 | 13 |
| β-strand | 344-348 | 5 | 13 |
| β-strand | 360-366 | 7 | 14 |
| β-strand | 385 | 1 | 15 |
| β-strand | 393 | 1 | 14 |
| β-strand | 397-400 | 4 | 13 |
| β-strand | 401 | 1 | 15 |
| α-helix | 403-404 | 2 | |
| β-strand | 408-417 | 10 | 14 |
| α-helix | 424-426 | 3 | |
| β-strand | 431-435 | 5 | 14 |
| β-strand | 447-452 | 6 | 16 |
| β-strand | 457-461 | 5 | 16 |
| α-helix | 462-464 | 3 | |
| β-strand | 471-480 | 10 | 17 |
| α-helix | 486-488 | 3 | |
| β-strand | 489-493 | 5 | 17 |
| β-strand | 497-499 | 3 | 16 |
| β-strand | 509-517 | 9 | 17 |
| β-strand | 521 | 1 | 17 |
| β-strand | 528-530 | 3 | 17 |
| α-helix | 531-533 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32-34 | 3 | 18 |
| β-strand | 46-47 | 2 | 19 |
| β-strand | 55-60 | 6 | 18 |
| β-strand | 66-72 | 7 | 18 |
| β-strand | 82-85 | 4 | 19 |
| α-helix | 86-88 | 3 | |
| β-strand | 89 | 1 | 19 |
| α-helix | 90 | 1 | |
| β-strand | 97-105 | 9 | 18 |
| β-strand | 121-128 | 8 | 19 |
| β-strand | 143-149 | 7 | 19 |
| β-strand | 166-173 | 8 | 18 |
| β-strand | 181-187 | 7 | 19 |
| β-strand | 192-201 | 10 | 18 |
| β-strand | 203-204 | 2 | 20 |
| β-strand | 208 | 1 | 21 |
| β-strand | 212-213 | 2 | 21 |
| β-strand | 217-218 | 2 | 20 |
| β-strand | 227 | 1 | 22 |
| β-strand | 230 | 1 | 22 |
| β-strand | 232-233 | 2 | 21 |
| β-strand | 244-247 | 4 | 22 |
| β-strand | 253-257 | 5 | 22 |
| α-helix | 260-263 | 4 | |
| β-strand | 266-268 | 3 | 23 |
| β-strand | 273-275 | 3 | 23 |
| α-helix | 276-277 | 2 | |
| β-strand | 280-281 | 2 | 24 |
| α-helix | 289-290 | 2 | |
| β-strand | 291-292 | 2 | 24 |
| α-helix | 293-294 | 2 | |
| α-helix | 298-301 | 4 | |
| β-strand | 304 | 1 | 24 |
| α-helix | 308-310 | 3 | |
| α-helix | 324-325 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-a receptor 4 | A, B | protein | 568 | HOMO SAPIENS | P54764 (AlphaFold model) |
>4BK4_1 EPHRIN TYPE-A RECEPTOR 4 (chains A, B) MGILPSPGMPALLSLVSLLSVLLMGCVAETGVTGSRVYPANEVTLLDSRSVQGELGWIAS PLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDC NSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNT EIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVE VRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDA TCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEW SSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTN YTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPN GVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPL EVTTNTVPSRIIGDGANSTGTKHHHHHH
Structurally Encoded Intraclass Differences in Epha Clusters Drive Distinct Cell Responses. Seiradake, E., Schaupp, A., Del Toro Ruiz, D. et al. Nat Struct Mol Biol (2013) 20:958. DOI 10.1038/NSMB.2617 · PubMed
Other PDB entries of the same protein (UniProt P54764 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4BK4 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.