Kappa variable light chain. Determined by X-ray diffraction at 2.06 Å resolution. Released 17 Jun 1999.
Explore 1QP1 in 3D Show helices and sheets RCSB PDB PDBe
1QP1 contains 10 α-helices and 33 β-strands across 3 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 |
|---|---|---|---|
| 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 | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-3 | 2 | |
| β-strand | 4-7 | 4 | 3 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 3 |
| β-strand | 70-75 | 6 | 3 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Bence-jones kappa I antibody bre (light chain) | A, B, C | protein | 107 | Homo sapiens | P01594 (AlphaFold model) |
>1QP1_1 BENCE-JONES KAPPA I ANTIBODY BRE (LIGHT CHAIN) (chains A, B, C) DIQMTQSPSSLSASVGDRVTITCQASQDISDYLIWYQQKLGKAPNLLIYDASTLETGVPS RFSGSGSGTEYTFTISSLQPEDIATYYCQQYDDLPYTFGQGTKVEIK
Molecular structure of the amyloid-forming protein kappa I Bre. Steinrauf, L.K., Chiang, M.Y., Shiuan, D. J Biochem (1999) 125:422-429. 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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