X-ray crystal structure of C3D: a C3 fragment and ligand for complement receptor 2. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Oct 1998.
Explore 1C3D in 3D Show helices and sheets RCSB PDB PDBe
1C3D contains 17 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 4-10 | 7 | |
| α-helix | 20-37 | 18 | |
| α-helix | 46-48 | 3 | |
| α-helix | 49-64 | 16 | |
| β-strand | 67 | 1 | 1 |
| β-strand | 73 | 1 | 1 |
| α-helix | 80-82 | 3 | |
| α-helix | 83-95 | 13 | |
| α-helix | 104-118 | 15 | |
| β-strand | 119 | 1 | 2 |
| β-strand | 125 | 1 | 2 |
| α-helix | 134-141 | 8 | |
| α-helix | 146-160 | 15 | |
| α-helix | 162-165 | 4 | |
| α-helix | 172-186 | 15 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-205 | 13 | |
| α-helix | 211-220 | 10 | |
| β-strand | 222 | 1 | 3 |
| β-strand | 226 | 1 | 3 |
| α-helix | 233-249 | 17 | |
| α-helix | 256-265 | 10 | |
| α-helix | 276-292 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C3D | A | protein | 294 | Homo sapiens | P01024 (AlphaFold model) |
>1C3D_1 C3D (chains A) MLDAERLKHLIVTPSGAGEQNMIGMTPTVIAVHYLDETEQWEKFGLEKRQGALELIKKGY TQQLAFRQPSSAFAAFVKRAPSTWLTAYVVKVFSLAVNLIAIDSQVLCGAVKWLILEKQK PDGVFQEDAPVIHQEMIGGLRNNNEKDMALTAFVLISLQEAKDICEEQVNSLPGSITKAG DFLEANYMNLQRSYTVAIAGYALAQMGRLKGPLLNKFLTTAKDKNRWEDPGKQLYNVEAT SYALLALLQLKDFDFVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDAP
X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2. Nagar, B., Jones, R.G., Diefenbach, R.J. et al. Science (1998) 280:1277-1281. DOI 10.1126/science.280.5367.1277 · PubMed
Other PDB entries of the same protein (UniProt P01024 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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