Gumby/Fam105B in complex with ubiquitin. Determined by X-ray diffraction at 2.4 Å resolution. Released 5 Jun 2013.
Explore 4KSK in 3D Show helices and sheets RCSB PDB PDBe
4KSK contains 46 α-helices and 34 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 | 82 | 1 | 1 |
| α-helix | 83-85 | 3 | |
| β-strand | 86-87 | 2 | 2 |
| α-helix | 88-95 | 8 | |
| α-helix | 101-114 | 14 | |
| β-strand | 117-121 | 5 | 2 |
| β-strand | 123 | 1 | 1 |
| α-helix | 129-140 | 12 | |
| α-helix | 147-150 | 4 | |
| α-helix | 152-154 | 3 | |
| α-helix | 157-164 | 8 | |
| α-helix | 166-170 | 5 | |
| α-helix | 184-202 | 19 | |
| α-helix | 208-216 | 9 | |
| α-helix | 223-248 | 26 | |
| α-helix | 255-261 | 7 | |
| α-helix | 269-272 | 4 | |
| α-helix | 273-277 | 5 | |
| β-strand | 280 | 1 | 3 |
| β-strand | 284 | 1 | 3 |
| α-helix | 288-298 | 11 | |
| β-strand | 301-306 | 6 | 4 |
| α-helix | 307-309 | 3 | |
| α-helix | 313-315 | 3 | |
| β-strand | 316-319 | 4 | 4 |
| β-strand | 329-336 | 8 | 4 |
| β-strand | 339-341 | 3 | 4 |
| β-strand | 342-345 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82 | 1 | 5 |
| α-helix | 83-85 | 3 | |
| β-strand | 86-87 | 2 | 6 |
| α-helix | 88-95 | 8 | |
| α-helix | 101-114 | 14 | |
| β-strand | 119-121 | 3 | 6 |
| α-helix | 122 | 1 | |
| β-strand | 123 | 1 | 5 |
| α-helix | 124 | 1 | |
| α-helix | 129-140 | 12 | |
| α-helix | 147-150 | 4 | |
| α-helix | 154-156 | 3 | |
| α-helix | 157-164 | 8 | |
| α-helix | 166-170 | 5 | |
| α-helix | 184-202 | 19 | |
| α-helix | 208-218 | 11 | |
| α-helix | 223-247 | 25 | |
| α-helix | 256-260 | 5 | |
| α-helix | 264-266 | 3 | |
| α-helix | 269-272 | 4 | |
| α-helix | 273-277 | 5 | |
| β-strand | 280 | 1 | 7 |
| β-strand | 284 | 1 | 7 |
| α-helix | 288-298 | 11 | |
| β-strand | 301-306 | 6 | 8 |
| α-helix | 307-309 | 3 | |
| β-strand | 316-319 | 4 | 8 |
| α-helix | 328 | 1 | |
| β-strand | 329-336 | 8 | 8 |
| β-strand | 339-341 | 3 | 8 |
| β-strand | 342-344 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 9 |
| β-strand | 12-17 | 6 | 9 |
| β-strand | 22 | 1 | 10 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 43-45 | 3 | 9 |
| β-strand | 48-49 | 2 | 9 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 10 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-69 | 4 | 9 |
| α-helix | 71-73 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-7 | 7 | 11 |
| β-strand | 12-17 | 6 | 11 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 43-45 | 3 | 11 |
| β-strand | 48-49 | 2 | 11 |
| α-helix | 50-51 | 2 | |
| β-strand | 65-69 | 5 | 11 |
| α-helix | 71-73 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein FAM105B | A, B | protein | 300 | Homo sapiens | Q96BN8 (AlphaFold model) |
| Polyubiquitin-C | C, D | protein | 80 | Homo sapiens | P0CG48 (AlphaFold model) |
>4KSK_1 Protein FAM105B (chains A, B) GSMYRAADEIEKEKELLIHERGASEPRLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEE VSQKFTSIRRVRGDNYSALRATLFQAMSQAVGLPPWLQDPELMLLPEKLISKYNWIKQWK LGLKFDGKNEDLVDKIKESLTLLRKKWAGLAEMRTAEARQIACDELFTNEAEEYSLYEAV KFLMLNRAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQVEMF LLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWPVVTLIAEDDRHYNIPVRVCEETSL
>4KSK_2 Polyubiquitin-C (chains C, D) GAMGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTL SDYNIQKESTLHLVLRLRGG
The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis. Rivkin, E., Almeida, S.M., Ceccarelli, D.F. et al. Nature (2013) 498:318-324. DOI 10.1038/nature12296 · PubMed
Other PDB entries of the same protein (UniProt Q96BN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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