Structure of the germline Vk1 O18/O8 light chain variable domain homodimer. Determined by X-ray diffraction at 1.3 Å resolution. Released 8 Apr 2008.
Explore 2Q20 in 3D Show helices and sheets RCSB PDB PDBe
2Q20 contains 9 α-helices and 22 β-strands across 2 chains. 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 | 1-3 | 3 | |
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-49 | 6 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 97 | 1 | |
| β-strand | 98 | 1 | 2 |
| α-helix | 99 | 1 | |
| β-strand | 102-106 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 0-3 | 4 | |
| β-strand | 4-7 | 4 | 3 |
| β-strand | 10-13 | 4 | 4 |
| β-strand | 19-25 | 7 | 3 |
| β-strand | 33-38 | 6 | 4 |
| β-strand | 45-49 | 5 | 4 |
| β-strand | 53-54 | 2 | 4 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 3 |
| β-strand | 70-75 | 6 | 3 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 4 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 4 |
| β-strand | 102-106 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vk1 O18/O8 germline light chain variable domain | A, B | protein | 109 | Homo sapiens | P01594 (AlphaFold model) |
>2Q20_1 Vk1 O18/O8 germline light chain variable domain (chains A, B) STDIQMTQSPSSLSASVGDRVTITCQASQDISNYLNWYQQKPGKAPKLLIYDASNLETGV PSRFSGSGSGTDFTFTISSLQPEDIATYYCQQYDNLPYTFGQGTKLEIK
Altered dimer interface decreases stability in an amyloidogenic protein. Baden, E.M., Owen, B.A., Peterson, F.C. et al. J Biol Chem (2008) 283:15853-15860. DOI 10.1074/jbc.M705347200 · PubMed
Other PDB entries of the same protein (UniProt P01594 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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