Crystal Structure of Arrestin2S and Clathrin. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Aug 2009.
Explore 3GC3 in 3D Show helices and sheets RCSB PDB PDBe
3GC3 contains 17 α-helices and 56 β-strands across 2 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 | 7-12 | 6 | 1 |
| β-strand | 19-22 | 4 | 1 |
| β-strand | 26-29 | 4 | 2 |
| β-strand | 34 | 1 | 2 |
| β-strand | 37-42 | 6 | 1 |
| β-strand | 52-63 | 12 | 3 |
| β-strand | 75-87 | 13 | 3 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-106 | 8 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 124-126 | 3 | |
| β-strand | 127-129 | 3 | 3 |
| β-strand | 140-151 | 12 | 3 |
| β-strand | 164-168 | 5 | 3 |
| β-strand | 169-172 | 4 | 2 |
| α-helix | 175-178 | 4 | |
| β-strand | 183-189 | 7 | 4 |
| β-strand | 196-203 | 8 | 4 |
| β-strand | 207-209 | 3 | 5 |
| β-strand | 214-222 | 9 | 4 |
| β-strand | 228-241 | 14 | 6 |
| β-strand | 247-258 | 12 | 6 |
| β-strand | 262 | 1 | 6 |
| β-strand | 266-274 | 9 | 4 |
| β-strand | 288-289 | 2 | 3 |
| β-strand | 300 | 1 | 3 |
| α-helix | 301-305 | 5 | |
| β-strand | 317-329 | 13 | 6 |
| β-strand | 335-341 | 7 | 6 |
| β-strand | 342-344 | 3 | 5 |
| α-helix | 345-348 | 4 | |
| β-strand | 370 | 1 | 7 |
| β-strand | 379-382 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 8 |
| α-helix | 15-18 | 4 | |
| α-helix | 22-24 | 3 | |
| β-strand | 30-34 | 5 | 9 |
| β-strand | 37-42 | 6 | 9 |
| β-strand | 49-54 | 6 | 9 |
| β-strand | 62-65 | 4 | 9 |
| β-strand | 66 | 1 | 7 |
| β-strand | 70-73 | 4 | 10 |
| β-strand | 79-84 | 6 | 10 |
| β-strand | 87-92 | 6 | 10 |
| β-strand | 97-103 | 7 | 10 |
| β-strand | 108-113 | 6 | 11 |
| β-strand | 118-123 | 6 | 11 |
| β-strand | 126-131 | 6 | 11 |
| α-helix | 136-138 | 3 | |
| β-strand | 139-143 | 5 | 11 |
| α-helix | 144-145 | 2 | |
| α-helix | 146-148 | 3 | |
| α-helix | 151 | 1 | |
| β-strand | 152-158 | 7 | 12 |
| β-strand | 164-172 | 9 | 12 |
| β-strand | 177-185 | 9 | 12 |
| β-strand | 190-194 | 5 | 12 |
| β-strand | 198-204 | 7 | 13 |
| β-strand | 213-222 | 10 | 13 |
| β-strand | 225-232 | 8 | 13 |
| α-helix | 241-245 | 5 | |
| β-strand | 246-249 | 4 | 13 |
| β-strand | 261-267 | 7 | 14 |
| β-strand | 272-277 | 6 | 14 |
| β-strand | 281-286 | 6 | 14 |
| β-strand | 292-297 | 6 | 14 |
| β-strand | 303-309 | 7 | 8 |
| α-helix | 310-312 | 3 | |
| β-strand | 314-319 | 6 | 8 |
| β-strand | 323-329 | 7 | 8 |
| α-helix | 334-336 | 3 | |
| α-helix | 337-341 | 5 | |
| α-helix | 345-355 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-arrestin-1 | A | protein | 385 | Bos taurus | P17870 (AlphaFold model) |
| Clathrin heavy chain 1 | B | protein | 363 | Bos taurus | P49951 (AlphaFold model) |
>3GC3_1 Beta-arrestin-1 (chains A) MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTCA FRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP PNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGP QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD ICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNL ASSTLLREGANREILGIIVSYKVKVKLVVSRGGDVAVELPFTLMHPKPKEEPPHREVPEH ETPVDTNLIELDTNDDDIVFEDFAR
>3GC3_2 Clathrin heavy chain 1 (chains B) MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSN PIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVA LVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGA MQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGN QPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISG ETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGA EEL
Structure of an arrestin2-clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking. Kang, D.S., Kern, R.C., Puthenveedu, M.A. et al. J Biol Chem (2009) 284:29860-29872. DOI 10.1074/jbc.M109.023366 · PubMed
Other PDB entries of the same protein (UniProt P17870 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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