HIV-2 CA pentamer; assembled via liposome templating. Determined by electron microscopy at 2.97 Å resolution. Released 5 Mar 2025.
Explore 9CNT in 3D Show helices and sheets RCSB PDB PDBe
9CNT contains 58 α-helices and 8 β-strands across 4 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 | 2-5 | 4 | 1 |
| β-strand | 9-12 | 4 | 1 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 64-83 | 20 | |
| α-helix | 90-91 | 2 | |
| α-helix | 95-98 | 4 | |
| α-helix | 100-104 | 5 | |
| α-helix | 110-117 | 8 | |
| α-helix | 126-145 | 20 | |
| α-helix | 161-174 | 14 | |
| α-helix | 179-187 | 9 | |
| α-helix | 189-192 | 4 | |
| α-helix | 196-204 | 9 | |
| α-helix | 211-217 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 2 |
| β-strand | 9-12 | 4 | 2 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-29 | 13 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-56 | 8 | |
| α-helix | 63-83 | 21 | |
| α-helix | 95-96 | 2 | |
| α-helix | 101-104 | 4 | |
| α-helix | 110-117 | 8 | |
| α-helix | 126-145 | 20 | |
| α-helix | 161-174 | 14 | |
| α-helix | 179-192 | 14 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 3 |
| β-strand | 12 | 1 | 3 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-29 | 13 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 65-83 | 19 | |
| α-helix | 90-91 | 2 | |
| α-helix | 96-98 | 3 | |
| α-helix | 100-104 | 5 | |
| α-helix | 110-117 | 8 | |
| α-helix | 126-145 | 20 | |
| α-helix | 161-175 | 15 | |
| α-helix | 179-192 | 14 | |
| α-helix | 196-201 | 6 | |
| α-helix | 211-217 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 4 |
| β-strand | 9-12 | 4 | 4 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-29 | 13 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 64-83 | 20 | |
| α-helix | 95-98 | 4 | |
| α-helix | 100-104 | 5 | |
| α-helix | 110-117 | 8 | |
| α-helix | 127-145 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-174 | 14 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-189 | 5 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Capsid protein p24 | A, B, C, D | protein | 240 | Human immunodeficiency virus 2 | P18042 |
>9CNT_1 Capsid protein p24 (chains A, B, C, D) PVQQTGGGNYIHVPLSPRTLNAWVKLVEDKKFGAEVVPGFQALSEGCTPYDINQMLNCVG DHQAAMQIIREIINDEAADWDAQHPIPGPLPAGQLRDPRGSDIAGTTSTVEEQIQWMYRP QNPVPVGNIYRRWIQIGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPA VKNWMTQTLLIQNANPDCKLVLKGLGMNPTLEEMLTACQGVGGPGQKARLMGSSHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| IHP | Inositol hexakisphosphate | C6 H18 O24 P6 | 2 |
Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM. Cook, M., Freniere, C., Wu, C. et al. Cell Rep (2025) 44:115245-115245. DOI 10.1016/j.celrep.2025.115245 · PubMed
Other PDB entries of the same protein (UniProt P18042), best resolution first:
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