crystal structure of the human EphA4 ectodomain in complex with human ephrin A5. Determined by X-ray diffraction at 5.3 Å resolution. Released 3 Jul 2013.
Explore 4BKA in 3D Show helices and sheets RCSB PDB PDBe
4BKA contains 17 α-helices and 63 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 | 31-34 | 4 | 1 |
| β-strand | 46-48 | 3 | 2 |
| β-strand | 55-56 | 2 | 1 |
| β-strand | 61 | 1 | 3 |
| β-strand | 65 | 1 | 3 |
| β-strand | 70-73 | 4 | 1 |
| β-strand | 82-85 | 4 | 2 |
| β-strand | 89-90 | 2 | 2 |
| β-strand | 97-104 | 8 | 1 |
| β-strand | 119 | 1 | 4 |
| β-strand | 122-129 | 8 | 2 |
| β-strand | 143-148 | 6 | 2 |
| β-strand | 168-173 | 6 | 1 |
| β-strand | 180-187 | 8 | 2 |
| β-strand | 190 | 1 | 4 |
| β-strand | 191-201 | 11 | 1 |
| β-strand | 204 | 1 | 5 |
| β-strand | 207-209 | 3 | 6 |
| β-strand | 212-214 | 3 | 6 |
| β-strand | 217 | 1 | 5 |
| β-strand | 227-230 | 4 | 7 |
| α-helix | 231-232 | 2 | |
| β-strand | 233 | 1 | 6 |
| α-helix | 234 | 1 | |
| β-strand | 237-238 | 2 | 8 |
| β-strand | 244-247 | 4 | 7 |
| β-strand | 253 | 1 | 7 |
| α-helix | 254-256 | 3 | |
| β-strand | 257 | 1 | 7 |
| β-strand | 261-262 | 2 | 8 |
| α-helix | 263 | 1 | |
| β-strand | 266-267 | 2 | 9 |
| β-strand | 274-275 | 2 | 9 |
| α-helix | 276-277 | 2 | |
| β-strand | 280-281 | 2 | 10 |
| β-strand | 291-292 | 2 | 10 |
| α-helix | 293-294 | 2 | |
| β-strand | 297 | 1 | 11 |
| β-strand | 304 | 1 | 10 |
| α-helix | 308 | 1 | |
| β-strand | 309 | 1 | 11 |
| α-helix | 310 | 1 | |
| β-strand | 314 | 1 | 12 |
| α-helix | 324-325 | 2 | |
| β-strand | 326 | 1 | 12 |
| α-helix | 327-332 | 6 | |
| β-strand | 335-339 | 5 | 13 |
| β-strand | 344-348 | 5 | 13 |
| β-strand | 360-366 | 7 | 14 |
| β-strand | 386 | 1 | 13 |
| β-strand | 393 | 1 | 14 |
| β-strand | 397-400 | 4 | 13 |
| β-strand | 408-417 | 10 | 14 |
| α-helix | 424-426 | 3 | |
| β-strand | 431-435 | 5 | 14 |
| α-helix | 439-441 | 3 | |
| β-strand | 447-448 | 2 | 15 |
| β-strand | 452 | 1 | 16 |
| β-strand | 457 | 1 | 16 |
| β-strand | 459-461 | 3 | 15 |
| α-helix | 462-464 | 3 | |
| β-strand | 471-478 | 8 | 17 |
| β-strand | 479-481 | 3 | 18 |
| β-strand | 489-493 | 5 | 17 |
| β-strand | 497-498 | 2 | 15 |
| β-strand | 508-511 | 4 | 18 |
| β-strand | 513-517 | 5 | 17 |
| β-strand | 528-531 | 4 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35-39 | 5 | 19 |
| α-helix | 45-49 | 5 | |
| β-strand | 53-56 | 4 | 20 |
| β-strand | 61-65 | 5 | 19 |
| β-strand | 81-85 | 5 | 20 |
| α-helix | 88-93 | 6 | |
| β-strand | 101-105 | 5 | 20 |
| β-strand | 117-121 | 5 | 19 |
| α-helix | 131-133 | 3 | |
| β-strand | 138-146 | 9 | 20 |
| β-strand | 157-163 | 7 | 20 |
| α-helix | 164-165 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-a receptor 4 | A | protein | 568 | HOMO SAPIENS | P54764 (AlphaFold model) |
| Ephrin-A5 | C | protein | 180 | HOMO SAPIENS | P52803 (AlphaFold model) |
>4BKA_1 EPHRIN TYPE-A RECEPTOR 4 (chains A) MGILPSPGMPALLSLVSLLSVLLMGCVAETGVTGSRVYPANEVTLLDSRSVQGELGWIAS PLEGGWEEVSIMDEKNTPIRTYQVCNVMEPSQNNWLRTDWITREGAQRVYIEIKFTLRDC NSLPGVMGTCKETFNLYYYESDNDKERFIRENQFVKIDTIAADESFTQVDIGDRIMKLNT EIRDVGPLSKKGFYLAFQDVGACIALVSVRVFYKKCPLTVRNLAQFPDTITGADTSSLVE VRGSCVNNSEEKDVPKMYCGADGEWLVPIGNCLCNAGHEERSGECQACKIGYYKALSTDA TCAKCPPHSYSVWEGATSCTCDRGFFRADNDAASMPCTRPPSAPLNLISNVNETSVNLEW SSPQNTGGRQDISYNVVCKKCGAGDPSKCRPCGSGVHYTPQQNGLKTTKVSITDLLAHTN YTFEIWAVNGVSKYNPNPDQSVSVTVTTNQAAPSSIALVQAKEVTRYSVALAWLEPDRPN GVILEYEVKYYEKDQNERSYRIVRTAARNTDIKGLNPLTSYVFHVRARTAAGYGDFSEPL EVTTNTVPSRIIGDGANSTGTKHHHHHH
>4BKA_2 EPHRIN-A5 (chains C) MGILPSPGMPALLSLVSLLSVLLMGCVAETGAVADRYAVYWNSSNPRFQRGDYHIDVCIN DYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFS EKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKGTKHHHHHH
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:
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