Clathrin terminal domain complexed with TLPWDLWTT. Determined by X-ray diffraction at 2.3 Å resolution. Released 25 Feb 2004.
Explore 1UTC in 3D Show helices and sheets RCSB PDB PDBe
1UTC contains 21 α-helices and 56 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 | 7-14 | 8 | 1 |
| α-helix | 15-18 | 4 | |
| α-helix | 22-24 | 3 | |
| β-strand | 30-31 | 2 | 2 |
| β-strand | 37-44 | 8 | 2 |
| β-strand | 47-54 | 8 | 2 |
| β-strand | 62-65 | 4 | 2 |
| β-strand | 70-73 | 4 | 3 |
| β-strand | 79-84 | 6 | 3 |
| β-strand | 87-92 | 6 | 3 |
| β-strand | 97-103 | 7 | 3 |
| β-strand | 110-113 | 4 | 4 |
| β-strand | 118-122 | 5 | 4 |
| β-strand | 126-131 | 6 | 4 |
| β-strand | 139-143 | 5 | 4 |
| α-helix | 144-145 | 2 | |
| α-helix | 146-148 | 3 | |
| α-helix | 151 | 1 | |
| β-strand | 152-158 | 7 | 5 |
| β-strand | 164-173 | 10 | 5 |
| β-strand | 176-185 | 10 | 5 |
| β-strand | 190-194 | 5 | 5 |
| β-strand | 198-204 | 7 | 6 |
| β-strand | 213-222 | 10 | 6 |
| β-strand | 225-232 | 8 | 6 |
| α-helix | 235-237 | 3 | |
| α-helix | 240-245 | 6 | |
| β-strand | 246-249 | 4 | 6 |
| β-strand | 261-267 | 7 | 7 |
| β-strand | 272-277 | 6 | 7 |
| β-strand | 281-286 | 6 | 7 |
| β-strand | 292-297 | 6 | 7 |
| β-strand | 303-309 | 7 | 1 |
| β-strand | 314-319 | 6 | 1 |
| β-strand | 323-329 | 7 | 1 |
| α-helix | 334-337 | 4 | |
| α-helix | 338-342 | 5 | |
| α-helix | 345-354 | 10 |
| 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 | 37-44 | 8 | 9 |
| β-strand | 47-54 | 8 | 9 |
| β-strand | 62-65 | 4 | 9 |
| 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 | 110-113 | 4 | 11 |
| β-strand | 118-122 | 5 | 11 |
| β-strand | 126-131 | 6 | 11 |
| 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 | 190-195 | 6 | 12 |
| β-strand | 198-204 | 7 | 13 |
| β-strand | 213-222 | 10 | 13 |
| β-strand | 225-232 | 8 | 13 |
| α-helix | 236-237 | 2 | |
| α-helix | 241-244 | 4 | |
| 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 |
| β-strand | 314-319 | 6 | 8 |
| β-strand | 323-329 | 7 | 8 |
| α-helix | 334-340 | 7 | |
| α-helix | 345-353 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clathrin heavy chain | A, B | protein | 363 | BOS TAURUS | P49951 (AlphaFold model) |
| Amphiphysin | P, Q | protein | 9 | HOMO SAPIENS | P49418 (AlphaFold model) |
>1UTC_1 CLATHRIN HEAVY CHAIN (chains A, B) MAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSN PIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVA LVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGA MQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGN QPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISG ETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGA EEL
>1UTC_2 AMPHIPHYSIN (chains P, Q) TLPWDLWTT
Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain beta-propeller. Miele, A.E., Watson, P.J., Evans, P.R. et al. Nat Struct Mol Biol (2004) 11:242-248. DOI 10.1038/nsmb736 · PubMed
Other PDB entries of the same protein (UniProt P49951 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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