2OEW: ALIX/AIP1 Bro1 Domain

Structure of ALIX/AIP1 Bro1 Domain. Determined by X-ray diffraction at 2.55 Å resolution. Released 27 Mar 2007.

Method
X-ray diffraction
Resolution
2.55 Å
Organism
Homo sapiens
Chains
1
Atoms
2,910
Mol. weight
42.74 kDa
Released
27 Mar 2007

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

Secondary structure: helices and β-sheets

2OEW contains 17 α-helices and 5 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: 17 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix8-114
β-strand1211
α-helix18-258
α-helix36-5015
α-helix51-555
α-helix62-7615
β-strand93-9641
β-strand10312
β-strand10712
β-strand110-11341
α-helix116-13621
α-helix143-17028
α-helix174-1763
α-helix177-1793
α-helix181-20525
α-helix210-23122
α-helix241-26626
α-helix270-29122
α-helix298-31417
α-helix315-3195
α-helix326-3283
α-helix330-3323

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Programmed cell death 6-interacting proteinAprotein380Homo sapiensQ8WUM4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2OEW_1 Programmed cell death 6-interacting protein (chains A)
MHHHHHHHHHHSGQNLYFQGHMATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQY
CRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAF
DKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGA
FLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQ
AADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQH
AAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVK
STPVNVPISQKFTDLFEKMV

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:

Browse structure collections

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