Vamp7 longin domain Hrb peptide complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Sept 2008.
Explore 2VX8 in 3D Show helices and sheets RCSB PDB PDBe
2VX8 contains 26 α-helices and 28 β-strands across 4 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 | 24-26 | 3 | 1 |
| α-helix | 27-31 | 5 | |
| β-strand | 48-53 | 6 | 2 |
| β-strand | 56-62 | 7 | 2 |
| β-strand | 66 | 1 | 3 |
| α-helix | 68-76 | 9 | |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 93-100 | 8 | 2 |
| β-strand | 103-110 | 8 | 2 |
| α-helix | 115-133 | 19 | |
| α-helix | 136-138 | 3 | |
| α-helix | 140-141 | 2 | |
| α-helix | 146-153 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 21-23 | 3 | |
| β-strand | 24-26 | 3 | 2 |
| α-helix | 28-31 | 4 | |
| α-helix | 32-34 | 3 | |
| β-strand | 40 | 1 | 3 |
| α-helix | 41-43 | 3 | |
| β-strand | 46-53 | 8 | 1 |
| β-strand | 56-62 | 7 | 1 |
| α-helix | 68-78 | 11 | |
| β-strand | 84-90 | 7 | 1 |
| β-strand | 93-100 | 8 | 1 |
| β-strand | 103-110 | 8 | 1 |
| α-helix | 118-133 | 16 | |
| α-helix | 134-138 | 5 | |
| α-helix | 146-156 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24-26 | 3 | 4 |
| α-helix | 28-31 | 4 | |
| α-helix | 32-34 | 3 | |
| β-strand | 40 | 1 | 5 |
| β-strand | 48-53 | 6 | 4 |
| β-strand | 56-62 | 7 | 4 |
| β-strand | 66 | 1 | 5 |
| α-helix | 68-76 | 9 | |
| β-strand | 84-90 | 7 | 4 |
| β-strand | 93-100 | 8 | 4 |
| β-strand | 103-110 | 8 | 4 |
| α-helix | 115-132 | 18 | |
| α-helix | 134-138 | 5 | |
| α-helix | 147-152 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24-26 | 3 | 6 |
| α-helix | 28-31 | 4 | |
| α-helix | 35-38 | 4 | |
| β-strand | 46-53 | 8 | 6 |
| β-strand | 56-62 | 7 | 6 |
| α-helix | 68-78 | 11 | |
| β-strand | 84-90 | 7 | 6 |
| β-strand | 93-100 | 8 | 6 |
| β-strand | 103-110 | 8 | 6 |
| α-helix | 118-133 | 16 | |
| α-helix | 136-139 | 4 | |
| α-helix | 146-155 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin-like protein rip, vesicle-associated membrane protein 7 | A, B, C, D | protein | 169 | HOMO SAPIENS, MUS MUSCULUS | P52594 (AlphaFold model), P70280 (AlphaFold model) |
>2VX8_1 NUCLEOPORIN-LIKE PROTEIN RIP, VESICLE-ASSOCIATED MEMBRANE PROTEIN 7 (chains A, B, C, D) GSVASVHASISGSSASSTSSTPEVKPLKSLLGDSAPTLHLNKGMAILFAVVARGTTILAK HAWCGGNFLEVTEQILAKIPSENNKLTYSHGNYLFHYICQDRIVYLCITDDDFERSRAFS FLNEVKKRFQTTYGSRAQTALPYAMNSEFSSVLAAQLKHHSENHHHHHH
Molecular Basis for the Sorting of the Snare Vamp7 Into Endocytic Clathrin-Coated Vesicles by the Arfgap Hrb. Pryor, P.R., Jackson, L., Gray, S.R. et al. Cell (2008) 134:817. DOI 10.1016/J.CELL.2008.07.023 · PubMed
Other PDB entries of the same protein (UniProt P52594 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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