Crystal structure of human CD59. Determined by X-ray diffraction at 2.12 Å resolution. Released 29 May 2007.
Explore 2OFS in 3D Show helices and sheets RCSB PDB PDBe
2OFS contains 2 α-helices 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 | 2-4 | 3 | 1 |
| β-strand | 16-18 | 3 | 1 |
| β-strand | 25-31 | 7 | 2 |
| β-strand | 34-40 | 7 | 2 |
| α-helix | 42-44 | 3 | |
| α-helix | 47-54 | 8 | |
| β-strand | 60-64 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CD59 glycoprotein | A | protein | 75 | Homo sapiens | P13987 (AlphaFold model) |
>2OFS_1 CD59 glycoprotein (chains A) FLQCYNCPNPTADCKTAVQCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENEL TYYCCKKDLCNFNEQ
Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex. Huang, Y., Fedarovich, A., Tomlinson, S. et al. Acta Crystallogr D Biol Crystallogr (2007) 63:714-721. DOI 10.1107/S0907444907015557 · 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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