Decameric damp complex of human serum amyloid P component. Determined by X-ray diffraction at 2.8 Å resolution. Released 24 Dec 1997.
Explore 1LGN in 3D Show helices and sheets RCSB PDB PDBe
1LGN contains 22 α-helices and 102 β-strands across 5 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 | 2 | 1 | 1 |
| β-strand | 7-11 | 5 | 2 |
| β-strand | 19-22 | 4 | 3 |
| β-strand | 30 | 1 | 4 |
| β-strand | 32-40 | 9 | 2 |
| β-strand | 47-54 | 8 | 3 |
| β-strand | 57-67 | 11 | 3 |
| β-strand | 70-75 | 6 | 3 |
| β-strand | 78-83 | 6 | 3 |
| β-strand | 92-99 | 8 | 2 |
| β-strand | 104-105 | 2 | 5 |
| β-strand | 106-109 | 4 | 2 |
| β-strand | 112-113 | 2 | 2 |
| β-strand | 117-118 | 2 | 5 |
| β-strand | 125 | 1 | 4 |
| β-strand | 129-133 | 5 | 3 |
| α-helix | 146-148 | 3 | |
| β-strand | 152-160 | 9 | 2 |
| α-helix | 166-174 | 9 | |
| α-helix | 177-180 | 4 | |
| β-strand | 183-184 | 2 | 2 |
| α-helix | 185-187 | 3 | |
| β-strand | 188 | 1 | 1 |
| β-strand | 190-193 | 4 | 3 |
| β-strand | 197-200 | 4 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 6 |
| β-strand | 7-11 | 5 | 7 |
| β-strand | 19-22 | 4 | 8 |
| β-strand | 30 | 1 | 9 |
| β-strand | 32-40 | 9 | 7 |
| β-strand | 47-54 | 8 | 8 |
| β-strand | 57-67 | 11 | 8 |
| β-strand | 70-75 | 6 | 8 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 92-99 | 8 | 7 |
| β-strand | 104-109 | 6 | 7 |
| β-strand | 112-113 | 2 | 7 |
| α-helix | 114-116 | 3 | |
| β-strand | 117-118 | 2 | 7 |
| β-strand | 125 | 1 | 9 |
| β-strand | 130-133 | 4 | 8 |
| α-helix | 146-148 | 3 | |
| β-strand | 152-160 | 9 | 7 |
| α-helix | 166-174 | 9 | |
| α-helix | 177-180 | 4 | |
| β-strand | 183-184 | 2 | 7 |
| α-helix | 185-187 | 3 | |
| β-strand | 188 | 1 | 6 |
| β-strand | 190-193 | 4 | 8 |
| β-strand | 197-200 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 10 |
| β-strand | 7-11 | 5 | 11 |
| β-strand | 19-22 | 4 | 12 |
| β-strand | 30 | 1 | 13 |
| β-strand | 32-40 | 9 | 11 |
| β-strand | 47-54 | 8 | 12 |
| β-strand | 57-67 | 11 | 12 |
| β-strand | 70-75 | 6 | 12 |
| β-strand | 78-83 | 6 | 12 |
| β-strand | 92-99 | 8 | 11 |
| β-strand | 104-107 | 4 | 11 |
| β-strand | 108-109 | 2 | 14 |
| β-strand | 112-113 | 2 | 14 |
| α-helix | 114-116 | 3 | |
| β-strand | 117-118 | 2 | 11 |
| β-strand | 125 | 1 | 13 |
| β-strand | 130-133 | 4 | 12 |
| α-helix | 146-148 | 3 | |
| β-strand | 152-160 | 9 | 11 |
| α-helix | 166-173 | 8 | |
| α-helix | 177-180 | 4 | |
| β-strand | 183-184 | 2 | 11 |
| α-helix | 185-187 | 3 | |
| β-strand | 188 | 1 | 10 |
| β-strand | 190-193 | 4 | 12 |
| β-strand | 197-200 | 4 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 15 |
| β-strand | 7-11 | 5 | 16 |
| β-strand | 19-22 | 4 | 17 |
| β-strand | 30 | 1 | 18 |
| β-strand | 32-40 | 9 | 16 |
| β-strand | 47-54 | 8 | 17 |
| β-strand | 57-67 | 11 | 17 |
| β-strand | 70-75 | 6 | 17 |
| β-strand | 78-83 | 6 | 17 |
| β-strand | 92-99 | 8 | 16 |
| β-strand | 104-109 | 6 | 16 |
| β-strand | 112-113 | 2 | 16 |
| β-strand | 117-118 | 2 | 16 |
| β-strand | 125 | 1 | 18 |
| β-strand | 130-133 | 4 | 17 |
| α-helix | 146-148 | 3 | |
| β-strand | 152-160 | 9 | 16 |
| α-helix | 166-174 | 9 | |
| α-helix | 177-180 | 4 | |
| β-strand | 183-184 | 2 | 16 |
| α-helix | 185-187 | 3 | |
| β-strand | 188 | 1 | 15 |
| β-strand | 190-193 | 4 | 17 |
| β-strand | 197-200 | 4 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serum amyloid P component | A, B, C, D, E | protein | 204 | Homo sapiens | P02743 (AlphaFold model) |
>1LGN_1 SERUM AMYLOID P COMPONENT (chains A, B, C, D, E) HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNE LLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLR QGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPA NILDWQALNYEIRGYVIIKPLVWV
Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. Hohenester, E., Hutchinson, W.L., Pepys, M.B. et al. J Mol Biol (1997) 269:570-578. DOI 10.1006/jmbi.1997.1075 · PubMed
Other PDB entries of the same protein (UniProt P02743 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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