Crystal structure of ALIX/AIP1. Determined by X-ray diffraction at 3.3 Å resolution. Released 27 Mar 2007.
Explore 2OEV in 3D Show helices and sheets RCSB PDB PDBe
2OEV contains 31 α-helices and 3 β-strands across 1 chain. 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 | 12 | 1 | 1 |
| α-helix | 19-28 | 10 | |
| α-helix | 35-37 | 3 | |
| α-helix | 43-54 | 12 | |
| α-helix | 63-76 | 14 | |
| α-helix | 79-81 | 3 | |
| β-strand | 93-96 | 4 | 1 |
| β-strand | 110-113 | 4 | 1 |
| α-helix | 116-137 | 22 | |
| α-helix | 143-164 | 22 | |
| α-helix | 167-170 | 4 | |
| α-helix | 174-176 | 3 | |
| α-helix | 181-205 | 25 | |
| α-helix | 210-229 | 20 | |
| α-helix | 241-266 | 26 | |
| α-helix | 270-290 | 21 | |
| α-helix | 298-314 | 17 | |
| α-helix | 315-319 | 5 | |
| α-helix | 321-325 | 5 | |
| α-helix | 326-328 | 3 | |
| α-helix | 330-332 | 3 | |
| α-helix | 361-398 | 38 | |
| α-helix | 415-425 | 11 | |
| α-helix | 430-469 | 40 | |
| α-helix | 481-484 | 4 | |
| α-helix | 487-514 | 28 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-533 | 7 | |
| α-helix | 535-536 | 2 | |
| α-helix | 547-575 | 29 | |
| α-helix | 581-590 | 10 | |
| α-helix | 596-607 | 12 | |
| α-helix | 609-639 | 31 | |
| α-helix | 645-696 | 52 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Programmed cell death 6-interacting protein | A | protein | 705 | Homo sapiens | Q8WUM4 (AlphaFold model) |
>2OEV_1 Programmed cell death 6-interacting protein (chains A) GIDPFTHMATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAA VGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLAL ASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSR EPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQY KDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQYYFGEEIARLQHAAELIKTVASRYDE YVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTD LFEKMVPVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTV PQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFK ERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAA IPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGV INEEALSVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVL KNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR
Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding. Fisher, R.D., Chung, H.Y., Zhai, Q. et al. Cell (2007) 128:841-852. DOI 10.1016/j.cell.2007.01.035 · PubMed
Other PDB entries of the same protein (UniProt Q8WUM4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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