Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Determined by solution NMR. Released 30 Sept 1994.
Explore 1CDQ in 3D Show helices and sheets RCSB PDB PDBe
1CDQ contains 1 α-helix and 5 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 | 2-3 | 2 | 1 |
| β-strand | 17-18 | 2 | 1 |
| β-strand | 25-30 | 6 | 2 |
| β-strand | 35-40 | 6 | 2 |
| α-helix | 50-53 | 4 | |
| β-strand | 62-64 | 3 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD59 | A | protein | 77 | Homo sapiens | P13987 (AlphaFold model) |
>1CDQ_1 CD59 (chains A) LQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELT YYCCKKDLCNFNEQLEN
Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Fletcher, C.M., Harrison, R.A., Lachmann, P.J. et al. Structure (1994) 2:185-199. DOI 10.1016/S0969-2126(00)00020-4 · PubMed
Other PDB entries of the same protein (UniProt P13987 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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