Clathrin Terminal Domain Complexed with Pitstop 1. Determined by X-ray diffraction at 1.7 Å resolution. Released 17 Aug 2011.
Explore 2XZG in 3D Show helices and sheets RCSB PDB PDBe
2XZG contains 10 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 | 235-237 | 3 | |
| 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 |
| β-strand | 314-319 | 6 | 1 |
| β-strand | 323-329 | 7 | 1 |
| α-helix | 334-340 | 7 | |
| α-helix | 345-356 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Clathrin heavy chain 1 | A | protein | 365 | HOMO SAPIENS | Q00610 (AlphaFold model) |
>2XZG_1 CLATHRIN HEAVY CHAIN 1 (chains A) FMAQILPIRFQEHLQLQNLGINPANIGFSTLTMESDKFICIREKVGEQAQVVIIDMNDPS NPIRRPISADSAIMNPASKVIALKAGKTLQIFNIEMKSKMKAHTMTDDVTFWKWISLNTV ALVTDNAVYHWSMEGESQPVKMFDRHSSLAGCQIINYRTDAKQKWLLLTGISAQQNRVVG AMQLYSVDRKVSQPIEGHAASFAQFKMEGNAEESTLFCFAVRGQAGGKLHIIEVGTPPTG NQPFPKKAVDVFFPPEAQNDFPVAMQISEKHDVVFLITKYGYIHLYDLETGTCIYMNRIS GETIFVTAPHEATAGIIGVNRKGQVLSVCVEEENIIPYITNVLQNPDLALRMAVRNNLAG AEELF
| ID | Name | Formula | Copies |
|---|---|---|---|
| VH1 | 2-(4-aminobenzyl)-1,3-dioxo-2,3-dihydro-1H-benzo[de]isoquinoline-5-sulfonate | C19 H13 N2 O5 S | 1 |
Water and common crystallization additives (ACT, GOL, 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. 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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