Solution structure of double super helix model. Determined by solution scattering. Released 7 Apr 2010.
Explore 3K2S in 3D Show helices and sheets RCSB PDB PDBe
3K2S contains 31 α-helices and 0 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 | 17-23 | 7 | |
| α-helix | 29-31 | 3 | |
| α-helix | 37-39 | 3 | |
| α-helix | 49-68 | 20 | |
| α-helix | 73-92 | 20 | |
| α-helix | 94-97 | 4 | |
| α-helix | 101-127 | 27 | |
| α-helix | 131-138 | 8 | |
| α-helix | 141-148 | 8 | |
| α-helix | 165-167 | 3 | |
| α-helix | 175-204 | 30 | |
| α-helix | 209-211 | 3 | |
| α-helix | 213-223 | 11 | |
| α-helix | 232-235 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-21 | 7 | |
| α-helix | 22-26 | 5 | |
| α-helix | 28-37 | 10 | |
| α-helix | 45-48 | 4 | |
| α-helix | 51-63 | 13 | |
| α-helix | 77-88 | 12 | |
| α-helix | 89-92 | 4 | |
| α-helix | 93-111 | 19 | |
| α-helix | 113-119 | 7 | |
| α-helix | 130-133 | 4 | |
| α-helix | 134-136 | 3 | |
| α-helix | 142-146 | 5 | |
| α-helix | 151-155 | 5 | |
| α-helix | 177-184 | 8 | |
| α-helix | 186-201 | 16 | |
| α-helix | 218-227 | 10 | |
| α-helix | 228-231 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Apolipoprotein A-I | A, B | protein | 243 | Homo sapiens | P02647 (AlphaFold model) |
>3K2S_1 Apolipoprotein A-I (chains A, B) DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKL REQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVE PLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEA LKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKL NTQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| POV | (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl… | C42 H82 N O8 P | 200 |
| CLR | Cholesterol | C27 H46 O | 20 |
Double superhelix model of high density lipoprotein. Wu, Z., Gogonea, V., Lee, X. et al. J Biol Chem (2009) 284:36605-36619. DOI 10.1074/jbc.M109.039537 · PubMed
Other PDB entries of the same protein (UniProt P02647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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