Clathrin terminal domain complexed with pitstop 2d. Determined by X-ray diffraction at 1.51 Å resolution. Released 26 Jun 2024.
Explore 9C0Z in 3D Show helices and sheets RCSB PDB PDBe
9C0Z contains 11 α-helices and 28 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 1 |
| α-helix | 15-18 | 4 | |
| α-helix | 22-24 | 3 | |
| β-strand | 30-34 | 5 | 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 |
| α-helix | 136-138 | 3 | |
| 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 | 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 |
| α-helix | 310-312 | 3 | |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clathrin heavy chain 1 | A | protein | 363 | Homo sapiens | Q00610 (AlphaFold model) |
>9C0Z_1 Clathrin heavy chain 1 (chains A) AQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPSNP IRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTVAL VTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVGAM QLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTGNQ PFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRISGE TIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAGAE ELF
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1ATQ | ~{N}-[4-oxidanylidene-5-[(2-phenoxyphenyl)methylidene]-1,3-thiazol-2-yl]naphtha… | C26 H18 N2 O4 S2 | 1 |
Water and common crystallization additives (GOL, EDO, ACT, PEG, TRS, DMS) are not listed.
Next-generation small molecule inhibitors of clathrin function acutely inhibit endocytosis. Horatscheck, A., Krauss, M., Bulut, H. et al. Structure (2025) 33:878. DOI 10.1016/j.str.2025.02.011 · PubMed
Other PDB entries of the same protein (UniProt Q00610 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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