Structure of a Human Bence-Jones Dimer Crystallized in U.S. Space Shuttle Mission STS-95: 100K. Determined by X-ray diffraction at 1.95 Å resolution. Released 1 Jul 2003.
Explore 1LGV in 3D Show helices and sheets RCSB PDB PDBe
1LGV contains 15 α-helices and 48 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 |
|---|---|---|---|
| β-strand | 4 | 1 | 1 |
| β-strand | 5 | 1 | 2 |
| β-strand | 9-12 | 4 | 3 |
| β-strand | 18-23 | 6 | 2 |
| β-strand | 35-40 | 6 | 3 |
| β-strand | 47-50 | 4 | 3 |
| β-strand | 51 | 1 | 4 |
| β-strand | 55 | 1 | 4 |
| β-strand | 64-69 | 6 | 2 |
| β-strand | 72-77 | 6 | 2 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 3 |
| β-strand | 100-102 | 3 | 3 |
| β-strand | 103 | 1 | 1 |
| β-strand | 106-110 | 5 | 3 |
| α-helix | 113-115 | 3 | |
| β-strand | 116 | 1 | 5 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 6 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 135-144 | 10 | 6 |
| β-strand | 145 | 1 | 5 |
| β-strand | 150-155 | 6 | 7 |
| β-strand | 158-159 | 2 | 7 |
| α-helix | 160 | 1 | |
| β-strand | 164-166 | 3 | 6 |
| α-helix | 167-169 | 3 | |
| β-strand | 170-171 | 2 | 6 |
| β-strand | 177-185 | 9 | 6 |
| α-helix | 187-191 | 5 | |
| β-strand | 196-202 | 7 | 7 |
| β-strand | 205-211 | 7 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 8 |
| β-strand | 9-12 | 4 | 9 |
| β-strand | 18-23 | 6 | 8 |
| α-helix | 25-27 | 3 | |
| β-strand | 35-40 | 6 | 9 |
| α-helix | 45-46 | 2 | |
| β-strand | 47-50 | 4 | 9 |
| β-strand | 51 | 1 | 10 |
| β-strand | 55 | 1 | 10 |
| β-strand | 64-69 | 6 | 8 |
| β-strand | 72-77 | 6 | 8 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-94 | 9 | 9 |
| β-strand | 99-102 | 4 | 9 |
| β-strand | 106-110 | 5 | 9 |
| β-strand | 116 | 1 | 11 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 12 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 135-144 | 10 | 12 |
| β-strand | 145 | 1 | 11 |
| β-strand | 150-155 | 6 | 13 |
| β-strand | 158-159 | 2 | 13 |
| β-strand | 164-166 | 3 | 12 |
| β-strand | 170-171 | 2 | 12 |
| β-strand | 177-185 | 9 | 12 |
| α-helix | 187-192 | 6 | |
| β-strand | 196-202 | 7 | 13 |
| β-strand | 205-211 | 7 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin lambda light chain | A, B | protein | 216 | Homo sapiens | Q6PJG0 (AlphaFold model) |
>1LGV_1 IMMUNOGLOBULIN LAMBDA LIGHT CHAIN (chains A, B) QTALTQPASVSGSPGQSITVSCTGVSSIVGSYNLVSWYQQHPGKAPKLLTYEVNKRPSGV SDRFSGSKSGNSASLTISGLQAEDEADYYCSSYDGSSTSVVFGGGTKLTVLGQPKAAPSV TLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTKPSKQSNNKYAAS SYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTAC
Comparison of the three-dimensional structures of a human Bence-Jones dimer crystallized on Earth and aboard US Space Shuttle Mission STS-95. Terzyan, S.S., DeWitt, C.R., Ramsland, P.A. et al. J Mol Recognit (2003) 16:83-90. DOI 10.1002/jmr.610 · PubMed
Other PDB entries of the same protein (UniProt Q6PJG0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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