7SNQ: Hexamer HIV-1 CA
Hexamer HIV-1 CA in complex with CPSF6 peptide and IP6 ligand. Determined by X-ray diffraction at 2.81 Å resolution. Released 7 Sept 2022.
- Method
- X-ray diffraction
- Resolution
- 2.81 Å
- Organisms
- Human immunodeficiency virus type 1 group M subtype B (isolate BH10), Human immunodeficiency virus 1
- Chains
- 24
- Atoms
- 20,569
- Mol. weight
- 326.86 kDa
- Ligands
- IHP
- Released
- 7 Sept 2022
Explore 7SNQ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7SNQ contains 189 α-helices and 28 β-strands across 23 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 | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-57 | 9 | |
| 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 | 161-175 | 15 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-190 | 6 | |
| α-helix | 191-192 | 2 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 | |
Chain B: 14 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 2 |
| β-strand | 10-12 | 3 | 2 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-57 | 9 | |
| α-helix | 63-83 | 21 | |
| β-strand | 96 | 1 | 3 |
| α-helix | 97-100 | 4 | |
| 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 | 185-192 | 8 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 | |
Chain C: 15 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 4 |
| β-strand | 10-12 | 3 | 4 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-29 | 13 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-57 | 9 | |
| α-helix | 63-83 | 21 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-144 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-174 | 14 | |
| α-helix | 179-184 | 6 | |
| α-helix | 185-190 | 6 | |
| α-helix | 191-192 | 2 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 | |
Chain D: 14 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 5 |
| β-strand | 10-12 | 3 | 5 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-57 | 9 | |
| α-helix | 63-83 | 21 | |
| α-helix | 97-100 | 4 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-119 | 9 | |
| α-helix | 126-144 | 19 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-175 | 15 | |
| α-helix | 189-192 | 4 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 | |
Chain E: 15 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 | 49-57 | 9 | |
| α-helix | 63-83 | 21 | |
| α-helix | 90-92 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-145 | 20 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-174 | 14 | |
| α-helix | 186-192 | 7 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 | |
Chain F: 14 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 7 |
| β-strand | 10-12 | 3 | 7 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-81 | 19 | |
| α-helix | 95 | 1 | |
| β-strand | 96 | 1 | 8 |
| α-helix | 97-100 | 4 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-119 | 9 | |
| α-helix | 126-144 | 19 | |
| α-helix | 161-175 | 15 | |
| α-helix | 180-192 | 13 | |
| α-helix | 196-205 | 10 | |
| α-helix | 211-217 | 7 | |
Chain G: 14 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 9 |
| β-strand | 10-12 | 3 | 9 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-57 | 9 | |
| α-helix | 63-83 | 21 | |
| α-helix | 97-99 | 3 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-145 | 20 | |
| α-helix | 150-152 | 3 | |
| α-helix | 161-174 | 14 | |
| α-helix | 186-192 | 7 | |
| α-helix | 196-203 | 8 | |
| α-helix | 211-217 | 7 | |
Chain H: 16 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 10 |
| β-strand | 10-12 | 3 | 10 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-30 | 14 | |
| α-helix | 36-43 | 8 | |
| α-helix | 49-57 | 9 | |
| α-helix | 63-81 | 19 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-119 | 9 | |
| α-helix | 126-145 | 20 | |
| 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 | |
8 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Capsid protein p24 | A, B, C, D, E, F, G, H, I, J, K, L | protein | 231 | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) | P03366 |
| Cleavage and polyadenylation specificity factor subunit 6 | M, N, O, P, Q, R, S, T, U, V, W, X | protein | 15 | Human immunodeficiency virus 1 | Q16630 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA
>7SNQ_1 Capsid protein p24 (chains A, B, C, D, E, F, G, H, I, J, K, L)
PIVQNLQGQMVHQCISPRTLNAWVKVVEEKAFSPEVIPMFSALSCGATPQDLNTMLNTVG
GHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH
NPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQE
VKNAATETLLVQNANPDCKTILKALGPGATLEEMMTACQGVGGPGHKARVL
Sequence of entity 2 (M, N, O, P, Q, R, S, T, U, V, W, X), FASTA
>7SNQ_2 Cleavage and polyadenylation specificity factor subunit 6 (chains M, N, O, P, Q, R, S, T, U, V, W, X)
PVLFPGQPFGQPPLG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| IHP | Inositol hexakisphosphate | C6 H18 O24 P6 | 4 |
Water and common crystallization additives (CL) are not listed.
Primary citation
Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection. Wei, G., Iqbal, N., Courouble, V.V. et al. Nat Commun (2022) 13:5879-5879. DOI 10.1038/s41467-022-33662-6 · PubMed
Other PDB entries of the same protein (UniProt P03366), best resolution first:
- 2HS1 0.84 Å, Ultra-high resolution X-ray crystal structure of HIV-1 protease V32I mutant with TMC114…
- 3NU3 1.02 Å, Wild Type HIV-1 Protease with Antiviral Drug Amprenavir
- 2IDW 1.1 Å, Crystal structure analysis of HIV-1 protease mutant V82A with a potent non-peptide…
- 4ZIP 1.11 Å, HIV-1 wild Type protease with GRL-0648A (a isophthalamide-derived P2-Ligand)
- 3NU6 1.16 Å, Crystal Structure of HIV-1 Protease Mutant I54M with Antiviral Drug Amprenavir
- 5JG1 1.16 Å, HIV-1 wild Type protease with GRL-031-14A (a Adamantane P1-Ligand with…
- 3NU4 1.2 Å, Crystal Structure of HIV-1 Protease Mutant V32I with Antiviral Drug Amprenavir
- 5AGZ 1.2 Å, Disubstituted bis-THF moieties as new P2 ligands in non-peptidal HIV- 1 Protease…
- 6PRF 1.21 Å, HIV-1 Protease multiple drug resistant clinical isolate mutant PR20 with GRL-14213A
- 2HS2 1.22 Å, Crystal structure of M46L mutant of HIV-1 protease complexed with TMC114 (darunavir)
- 5AH8 1.26 Å, Disubstituted bis-THF moieties as new P2 ligands in non-peptidal HIV- 1 Protease…
- 3OK9 1.27 Å, Crystal structure of wild-type HIV-1 protease with new oxatricyclic designed inhibitor…
Browse structure collections
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