Clathrin terminal domain complexed with pitstop 2. Determined by X-ray diffraction at 1.69 Å resolution. Released 1 Aug 2012.
Explore 4G55 in 3D Show helices and sheets RCSB PDB PDBe
4G55 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 | 108-113 | 6 | 4 |
| β-strand | 118-123 | 6 | 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 | 246-250 | 5 | 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 | 369 | Homo sapiens | Q00610 (AlphaFold model) |
>4G55_1 Clathrin heavy chain 1 (chains A) GSPEFMAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDM NDPSNPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWIS LNTVALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQN RVVGAMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGT PPTGNQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYM NRISGETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRN NLAGAEELF
| ID | Name | Formula | Copies |
|---|---|---|---|
| VH2 | N-[5-[(4-bromophenyl)methyl]-4-hydroxy-1,3-thiazol-2-yl]naphthalene-1-sulfonami… | C20 H15 Br N2 O3 S2 | 1 |
Water and common crystallization additives (DMS, ACT, EDO, PEG) are not listed.
Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. von Kleist, L., Stahlschmidt, W., Bulut, H. et al. Cell (2011) 146:471-484. DOI 10.1016/j.cell.2011.06.025 · 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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