Crystal structure of HIV-1 capsid N-terminal domain in complex with NUP358 cyclophilin. Determined by X-ray diffraction at 1.95 Å resolution. Released 14 Aug 2013.
Explore 4LQW in 3D Show helices and sheets RCSB PDB PDBe
4LQW contains 27 α-helices and 30 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 | 5-12 | 8 | 1 |
| β-strand | 15-24 | 10 | 1 |
| α-helix | 30-41 | 12 | |
| β-strand | 52 | 1 | 1 |
| β-strand | 55-57 | 3 | 1 |
| β-strand | 61-64 | 4 | 1 |
| β-strand | 77 | 1 | 2 |
| β-strand | 80 | 1 | 2 |
| β-strand | 83 | 1 | 3 |
| β-strand | 97-100 | 4 | 1 |
| β-strand | 108 | 1 | 3 |
| β-strand | 112-115 | 4 | 1 |
| α-helix | 120-122 | 3 | |
| β-strand | 128-134 | 7 | 1 |
| α-helix | 136-143 | 8 | |
| β-strand | 156-163 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-12 | 8 | 4 |
| β-strand | 15-24 | 10 | 4 |
| α-helix | 30-41 | 12 | |
| β-strand | 52 | 1 | 4 |
| β-strand | 55-57 | 3 | 4 |
| β-strand | 61-64 | 4 | 4 |
| β-strand | 77 | 1 | 5 |
| β-strand | 80 | 1 | 5 |
| β-strand | 83 | 1 | 6 |
| β-strand | 97-100 | 4 | 4 |
| β-strand | 108 | 1 | 6 |
| β-strand | 112-115 | 4 | 4 |
| α-helix | 120-122 | 3 | |
| β-strand | 128-134 | 7 | 4 |
| α-helix | 136-144 | 9 | |
| β-strand | 156-163 | 8 | 4 |
| 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 | 36-42 | 7 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 85-88 | 4 | |
| α-helix | 90-92 | 3 | |
| α-helix | 97-100 | 4 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-118 | 8 | |
| α-helix | 126-145 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 8 |
| β-strand | 11-12 | 2 | 8 |
| α-helix | 14-16 | 3 | |
| α-helix | 17-29 | 13 | |
| α-helix | 36-42 | 7 | |
| α-helix | 49-58 | 10 | |
| α-helix | 63-83 | 21 | |
| α-helix | 90-92 | 3 | |
| α-helix | 97-100 | 4 | |
| α-helix | 101-104 | 4 | |
| α-helix | 111-119 | 9 | |
| α-helix | 126-143 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 SUMO-protein ligase RanBP2 | A, B | protein | 177 | Homo sapiens | P49792 |
| Capsid protein p24 | C, D | protein | 146 | Human immunodeficiency virus type 1 | P12497 |
>4LQW_1 E3 SUMO-protein ligase RanBP2 (chains A, B) MAHHHHHHMELSKETNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGFG FKNSIFHRVIPDFVCQGGDITKHDGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNT NNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITITECGQI
>4LQW_2 Capsid protein p24 (chains C, D) PIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVG GHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTH NPPIPVGEIYKRWIILGLNKIVRMYS
HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358. Bichel, K., Price, A.J., Schaller, T. et al. Retrovirology (2013) 10:81-81. DOI 10.1186/1742-4690-10-81 · PubMed
Other PDB entries of the same protein (UniProt P49792), best resolution first:
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