Crystal structure of the complete EphA2 ectodomain in complex with ephrin A5 receptor binding domain. Determined by X-ray diffraction at 4.83 Å resolution. Released 16 Mar 2010.
Explore 2X11 in 3D Show helices and sheets RCSB PDB PDBe
2X11 contains 21 α-helices and 62 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 | 28-33 | 6 | 1 |
| α-helix | 34-36 | 3 | |
| β-strand | 44-46 | 3 | 2 |
| β-strand | 53-59 | 7 | 1 |
| β-strand | 62-70 | 9 | 1 |
| β-strand | 79-82 | 4 | 2 |
| α-helix | 83-85 | 3 | |
| β-strand | 86-87 | 2 | 2 |
| β-strand | 94-102 | 9 | 1 |
| β-strand | 103 | 1 | 3 |
| α-helix | 105-107 | 3 | |
| β-strand | 116 | 1 | 4 |
| β-strand | 119-126 | 8 | 2 |
| α-helix | 136-138 | 3 | |
| α-helix | 139 | 1 | |
| β-strand | 140-145 | 6 | 2 |
| β-strand | 151 | 1 | 3 |
| α-helix | 154-157 | 4 | |
| β-strand | 164-170 | 7 | 1 |
| β-strand | 177-184 | 8 | 2 |
| β-strand | 187 | 1 | 4 |
| β-strand | 188-199 | 12 | 1 |
| β-strand | 200-201 | 2 | 5 |
| α-helix | 202-203 | 2 | |
| β-strand | 204-206 | 3 | 6 |
| β-strand | 209-211 | 3 | 6 |
| β-strand | 214-215 | 2 | 5 |
| α-helix | 216-217 | 2 | |
| β-strand | 224-227 | 4 | 7 |
| β-strand | 229-230 | 2 | 6 |
| α-helix | 231 | 1 | |
| β-strand | 234-235 | 2 | 8 |
| β-strand | 244-247 | 4 | 7 |
| β-strand | 253 | 1 | 7 |
| β-strand | 257 | 1 | 7 |
| β-strand | 261-262 | 2 | 8 |
| β-strand | 266-269 | 4 | 9 |
| β-strand | 272-275 | 4 | 9 |
| α-helix | 276-277 | 2 | |
| β-strand | 280-281 | 2 | 10 |
| α-helix | 290 | 1 | |
| β-strand | 291-292 | 2 | 10 |
| α-helix | 293 | 1 | |
| β-strand | 297-298 | 2 | 11 |
| α-helix | 300-301 | 2 | |
| α-helix | 307 | 1 | |
| β-strand | 308-309 | 2 | 11 |
| α-helix | 310 | 1 | |
| β-strand | 314 | 1 | 12 |
| α-helix | 324-325 | 2 | |
| β-strand | 326 | 1 | 12 |
| β-strand | 332 | 1 | 13 |
| β-strand | 335-338 | 4 | 14 |
| β-strand | 344-348 | 5 | 14 |
| β-strand | 351 | 1 | 13 |
| β-strand | 361-369 | 9 | 15 |
| β-strand | 376-378 | 3 | 15 |
| α-helix | 379-380 | 2 | |
| β-strand | 384-385 | 2 | 14 |
| β-strand | 392 | 1 | 15 |
| β-strand | 396-400 | 5 | 14 |
| β-strand | 407-415 | 9 | 15 |
| α-helix | 419-421 | 3 | |
| β-strand | 427-431 | 5 | 15 |
| β-strand | 441-446 | 6 | 16 |
| β-strand | 453-457 | 5 | 16 |
| α-helix | 460-463 | 4 | |
| β-strand | 468-475 | 8 | 17 |
| β-strand | 482-487 | 6 | 17 |
| β-strand | 491-493 | 3 | 16 |
| β-strand | 502-510 | 9 | 17 |
| β-strand | 517-518 | 2 | 17 |
| β-strand | 522-525 | 4 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 35-39 | 5 | 18 |
| α-helix | 45-48 | 4 | |
| β-strand | 53-56 | 4 | 19 |
| β-strand | 61-65 | 5 | 18 |
| β-strand | 81-86 | 6 | 19 |
| α-helix | 88-93 | 6 | |
| β-strand | 100-106 | 7 | 19 |
| β-strand | 117-121 | 5 | 18 |
| β-strand | 138-146 | 9 | 19 |
| β-strand | 158-163 | 6 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ephrin type-a receptor 2 | A | protein | 545 | Homo sapiens | P29317 (AlphaFold model) |
| Ephrin-A5 | B | protein | 177 | Homo sapiens | P52803 (AlphaFold model) |
>2X11_1 EPHRIN TYPE-A RECEPTOR 2 (chains A) MGILPSPGMPALLSLVSLLSVLLMGCVAKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNI MNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKET FNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGF YLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPP GGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTL PSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGRE DIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGV SGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGD SNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNGTKH HHHHH
>2X11_2 EPHRIN-A5 (chains B) MGILPSPGMPALLSLVSLLSVLLMGCVAAVADRYAVYWNSSNPRFQRGDYHIDVCINDYL DVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKF QLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKGTKHHHHHH
An Extracellular Steric Seeding Mechanism for Eph-Ephrin Signalling Platform Assembly. Seiradake, E., Harlos, K., Sutton, G. et al. Nat Struct Mol Biol (2010) 17:398. DOI 10.1038/NSMB.1782 · PubMed
Other PDB entries of the same protein (UniProt P29317 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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