2OEV: ALIX/AIP1

Crystal structure of ALIX/AIP1. Determined by X-ray diffraction at 3.3 Å resolution. Released 27 Mar 2007.

Method
X-ray diffraction
Resolution
3.3 Å
Organism
Homo sapiens
Chains
1
Atoms
5,486
Mol. weight
78.97 kDa
Released
27 Mar 2007

Explore 2OEV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 31 helices, 3 β-strands

ElementResiduesLengthSheet
β-strand1211
α-helix19-2810
α-helix35-373
α-helix43-5412
α-helix63-7614
α-helix79-813
β-strand93-9641
β-strand110-11341
α-helix116-13722
α-helix143-16422
α-helix167-1704
α-helix174-1763
α-helix181-20525
α-helix210-22920
α-helix241-26626
α-helix270-29021
α-helix298-31417
α-helix315-3195
α-helix321-3255
α-helix326-3283
α-helix330-3323
α-helix361-39838
α-helix415-42511
α-helix430-46940
α-helix481-4844
α-helix487-51428
α-helix517-5237
α-helix527-5337
α-helix535-5362
α-helix547-57529
α-helix581-59010
α-helix596-60712
α-helix609-63931
α-helix645-69652

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Programmed cell death 6-interacting proteinAprotein705Homo sapiensQ8WUM4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2OEV_1 Programmed cell death 6-interacting protein (chains A)
GIDPFTHMATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAA
VGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLAL
ASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSR
EPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQY
KDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQYYFGEEIARLQHAAELIKTVASRYDE
YVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTD
LFEKMVPVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTV
PQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFK
ERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAA
IPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGV
INEEALSVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVL
KNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFAR

Primary citation

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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