8CL0: Gag polyprotein
HIV-1 mature capsid hexamer next to pentamer (type I) from CA-IP6 CLPs bound to Nup153 peptide. Determined by electron microscopy at 3.12 Å resolution. Released 26 Apr 2023.
- Method
- Electron microscopy
- Resolution
- 3.12 Å
- Organisms
- Human immunodeficiency virus 1, Homo sapiens
- Chains
- 12
- Atoms
- 10,387
- Mol. weight
- 164.7 kDa
- Released
- 26 Apr 2023
Explore 8CL0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8CL0 contains 97 α-helices and 12 β-strands across 6 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.
Chain A: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 1 |
| β-strand | 10-12 | 3 | 1 |
| α-helix | 13-16 | 4 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 96-100 | 5 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-144 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-175 | 15 | |
| 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 | |
Chain B: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 2 |
| β-strand | 10-12 | 3 | 2 |
| α-helix | 13-16 | 4 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-144 | 19 | |
| α-helix | 161-175 | 15 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-189 | 5 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-203 | 8 | |
| α-helix | 211-217 | 7 | |
Chain C: 17 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 3 |
| β-strand | 10-12 | 3 | 3 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-44 | 9 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 85-87 | 3 | |
| α-helix | 97-100 | 4 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-144 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-175 | 15 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-189 | 5 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-204 | 9 | |
| α-helix | 211-218 | 8 | |
Chain D: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 4 |
| β-strand | 10-12 | 3 | 4 |
| α-helix | 13-16 | 4 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 96-100 | 5 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-119 | 9 | |
| α-helix | 126-144 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 155-156 | 2 | |
| α-helix | 161-175 | 15 | |
| α-helix | 179-192 | 14 | |
| α-helix | 196-204 | 9 | |
| α-helix | 211-218 | 8 | |
Chain E: 18 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 5 |
| β-strand | 10-12 | 3 | 5 |
| α-helix | 13-16 | 4 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-144 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 155-156 | 2 | |
| α-helix | 161-175 | 15 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-189 | 5 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-204 | 9 | |
| α-helix | 206 | 1 | |
| α-helix | 211-217 | 7 | |
Chain F: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 6 |
| β-strand | 10-12 | 3 | 6 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 96-100 | 5 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-119 | 9 | |
| α-helix | 126-145 | 20 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-175 | 15 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-189 | 5 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-203 | 8 | |
| α-helix | 211-218 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Gag polyprotein | A, B, C, D, E, F | protein | 232 | Human immunodeficiency virus 1 | P12493 |
| Nuclear pore complex protein Nup153 | G, H, I, J, K, L | protein | 17 | Homo sapiens | P49790 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>8CL0_1 Gag polyprotein (chains A, B, C, D, E, F)
MPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTV
GGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMT
HNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQ
EVKNWMTETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVL
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>8CL0_2 Nuclear pore complex protein Nup153 (chains G, H, I, J, K, L)
TNNSPSGVFTFGANSST
Primary citation
Two structural switches in HIV-1 capsid regulate capsid curvature and host factor binding. Stacey, J.C.V., Tan, A., Lu, J.M. et al. Proc Natl Acad Sci U S A (2023) 120:e2220557120-e2220557120. DOI 10.1073/pnas.2220557120 · PubMed
Other PDB entries of the same protein (UniProt P12493), best resolution first:
- 8QUK 1.38 Å, Hexameric HIV-1 CA in complex with DDD00100439
- 8QUH 1.55 Å, Hexameric HIV-1 CA in complex with DDD00057456
- 8FIU 1.56 Å, Potent long-acting inhibitors targeting HIV-1 capsid based on a versatile…
- 8QUB 1.63 Å, Hexameric HIV-1 CA in complex with DDD00074110
- 8QUJ 1.63 Å, Hexameric HIV-1 CA in complex with DDD00100452
- 8QUL 1.67 Å, Hexameric HIV-1 CA in complex with DDD00100555
- 8QUI 1.69 Å, Hexameric HIV-1 CA in complex with DDD00024969
- 5JPA 1.7 Å, Hexameric HIV-1 CA H12Y mutant
- 8QV9 1.76 Å, Hexameric HIV-1 CA in complex with DDD01829021
- 4U0C 1.77 Å, Hexameric HIV-1 CA in complex with Nup153 peptide, P6 crystal form
- 8VRP 1.8 Å, HIV-CA Disulfide linked Hexamer bound to 4-Quinazolinone Scaffold inhibitor
- 8QUY 1.88 Å, Hexameric HIV-1 CA in complex with DDD01728501
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