Crystal structure of unliganded human CD21 SCR1-SCR2 (Complement receptor type 2). Determined by X-ray diffraction at 1.8 Å resolution. Released 5 Jul 2002.
Explore 1LY2 in 3D Show helices and sheets RCSB PDB PDBe
1LY2 contains 5 α-helices and 18 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 |
| α-helix | 5-8 | 4 | |
| β-strand | 12-14 | 3 | 2 |
| β-strand | 21-22 | 2 | 1 |
| β-strand | 26-28 | 3 | 3 |
| β-strand | 29-31 | 3 | 2 |
| β-strand | 35-38 | 4 | 4 |
| β-strand | 42-44 | 3 | 3 |
| β-strand | 45-46 | 2 | 5 |
| β-strand | 54-55 | 2 | 5 |
| β-strand | 61-64 | 4 | 4 |
| α-helix | 65 | 1 | |
| β-strand | 70-71 | 2 | 6 |
| α-helix | 72-74 | 3 | |
| β-strand | 79-83 | 5 | 7 |
| β-strand | 88-89 | 2 | 6 |
| β-strand | 93-98 | 6 | 7 |
| α-helix | 99 | 1 | |
| β-strand | 102-105 | 4 | 8 |
| β-strand | 109-112 | 4 | 7 |
| β-strand | 118-119 | 2 | 7 |
| α-helix | 122-124 | 3 | |
| β-strand | 125-128 | 4 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| complement receptor type 2 | A | protein | 130 | Homo sapiens | P20023 (AlphaFold model) |
>1LY2_1 complement receptor type 2 (chains A) EASCGSPPPILNGRISYYSTPIAVGTVIRYSCSGTFRLIGEKSLLCITKDKVDGTWDKPA PKCEYFNKYSSCPEPIVPGGYKIRGSTPYRHGDSVTFACKTNFSMNGNKSVWCQANNMWG PTRLPTCVSI
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
The crystal structure of human CD21: Implications for Epstein-Barr virus and C3d binding. Prota, A.E., Sage, D.R., Stehle, T. et al. Proc Natl Acad Sci U S A (2002) 99:10641-10646. DOI 10.1073/pnas.162360499 · PubMed
Other PDB entries of the same protein (UniProt P20023 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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