4NEE: AP-2 alpha/simga2 complex
crystal structure of AP-2 alpha/simga2 complex bound to HIV-1 Nef. Determined by X-ray diffraction at 2.88 Å resolution. Released 29 Jan 2014.
- Method
- X-ray diffraction
- Resolution
- 2.88 Å
- Organisms
- Rattus norvegicus, Human immunodeficiency virus 1
- Chains
- 12
- Atoms
- 21,530
- Mol. weight
- 316.4 kDa
- Released
- 29 Jan 2014
Explore 4NEE in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4NEE contains 172 α-helices and 70 β-strands across 12 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: 23 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-21 | 11 | |
| α-helix | 26-44 | 19 | |
| α-helix | 52-67 | 16 | |
| α-helix | 76-84 | 9 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 127-138 | 12 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-156 | 7 | |
| α-helix | 162-178 | 17 | |
| α-helix | 188-195 | 8 | |
| α-helix | 201-217 | 17 | |
| α-helix | 220-222 | 3 | |
| α-helix | 224-238 | 15 | |
| β-strand | 248-249 | 2 | 14 |
| β-strand | 252-253 | 2 | 14 |
| α-helix | 255-265 | 11 | |
| α-helix | 274-292 | 19 | |
| α-helix | 294-295 | 2 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-338 | 15 | |
| α-helix | 343-356 | 14 | |
| α-helix | 363-367 | 5 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-395 | 13 | |
Chain B: 28 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-22 | 12 | |
| α-helix | 26-44 | 19 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-67 | 16 | |
| α-helix | 76-84 | 9 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 125-138 | 14 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-156 | 7 | |
| α-helix | 162-178 | 17 | |
| α-helix | 180-182 | 3 | |
| α-helix | 188-194 | 7 | |
| α-helix | 195-197 | 3 | |
| α-helix | 201-217 | 17 | |
| α-helix | 219-222 | 4 | |
| α-helix | 224-237 | 14 | |
| α-helix | 245-247 | 3 | |
| β-strand | 248-249 | 2 | 12 |
| β-strand | 252-253 | 2 | 12 |
| α-helix | 255-265 | 11 | |
| α-helix | 274-292 | 19 | |
| α-helix | 294-295 | 2 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-338 | 15 | |
| α-helix | 343-356 | 14 | |
| α-helix | 363-366 | 4 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-395 | 13 | |
Chain C: 11 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 56-60 | 5 | |
| α-helix | 75-76 | 2 | |
| α-helix | 81-93 | 13 | |
| α-helix | 100 | 1 | |
| β-strand | 101 | 1 | 24 |
| α-helix | 102 | 1 | |
| α-helix | 104-118 | 15 | |
| β-strand | 127 | 1 | 25 |
| β-strand | 134 | 1 | 24 |
| β-strand | 136 | 1 | 25 |
| β-strand | 143-147 | 5 | 24 |
| α-helix | 148-149 | 2 | |
| α-helix | 150-156 | 7 | |
| β-strand | 163 | 1 | 2 |
| β-strand | 181-185 | 5 | 24 |
| α-helix | 188-191 | 4 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
Chain D: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 1 |
| β-strand | 14-19 | 6 | 1 |
| α-helix | 25-41 | 17 | |
| β-strand | 49-51 | 3 | 1 |
| β-strand | 55-62 | 8 | 1 |
| β-strand | 65-72 | 8 | 1 |
| α-helix | 77-95 | 19 | |
| β-strand | 99 | 1 | 2 |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 3 |
| β-strand | 122-123 | 2 | 3 |
| α-helix | 128-140 | 13 | |
Chain E: 12 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-60 | 4 | |
| α-helix | 75-76 | 2 | |
| β-strand | 77 | 1 | 15 |
| α-helix | 81-94 | 14 | |
| α-helix | 100 | 1 | |
| β-strand | 101 | 1 | 16 |
| α-helix | 102 | 1 | |
| α-helix | 104-118 | 15 | |
| β-strand | 120 | 1 | 15 |
| β-strand | 127 | 1 | 17 |
| β-strand | 134 | 1 | 16 |
| β-strand | 136 | 1 | 17 |
| β-strand | 143-147 | 5 | 16 |
| α-helix | 148-149 | 2 | |
| α-helix | 150-157 | 8 | |
| α-helix | 167-170 | 4 | |
| β-strand | 181-185 | 5 | 16 |
| α-helix | 188-191 | 4 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
Chain F: 5 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 6 |
| β-strand | 14-19 | 6 | 6 |
| α-helix | 25-41 | 17 | |
| β-strand | 49-51 | 3 | 6 |
| β-strand | 55-62 | 8 | 6 |
| β-strand | 65-72 | 8 | 6 |
| α-helix | 77-95 | 19 | |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 7 |
| β-strand | 122-123 | 2 | 7 |
| α-helix | 128-140 | 13 | |
Chain G: 27 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-22 | 12 | |
| α-helix | 26-45 | 20 | |
| α-helix | 49-51 | 3 | |
| α-helix | 52-67 | 16 | |
| α-helix | 76-83 | 8 | |
| α-helix | 88-100 | 13 | |
| α-helix | 106-121 | 16 | |
| α-helix | 125-138 | 14 | |
| α-helix | 141-147 | 7 | |
| α-helix | 150-156 | 7 | |
| α-helix | 162-178 | 17 | |
| α-helix | 188-193 | 6 | |
| α-helix | 194-197 | 4 | |
| α-helix | 201-217 | 17 | |
| α-helix | 220-222 | 3 | |
| α-helix | 224-238 | 15 | |
| α-helix | 243-247 | 5 | |
| β-strand | 248-249 | 2 | 11 |
| β-strand | 252-253 | 2 | 11 |
| α-helix | 255-265 | 11 | |
| α-helix | 274-292 | 19 | |
| α-helix | 294-295 | 2 | |
| α-helix | 300-320 | 21 | |
| α-helix | 324-338 | 15 | |
| α-helix | 343-358 | 16 | |
| α-helix | 363-366 | 4 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-379 | 10 | |
| α-helix | 383-395 | 13 | |
Chain H: 11 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-64 | 8 | |
| β-strand | 77 | 1 | 18 |
| α-helix | 81-93 | 13 | |
| α-helix | 100 | 1 | |
| β-strand | 101 | 1 | 19 |
| α-helix | 102 | 1 | |
| α-helix | 104-118 | 15 | |
| β-strand | 120 | 1 | 18 |
| β-strand | 127 | 1 | 20 |
| β-strand | 134 | 1 | 19 |
| β-strand | 136 | 1 | 20 |
| β-strand | 143-147 | 5 | 19 |
| α-helix | 148-149 | 2 | |
| α-helix | 150-156 | 7 | |
| β-strand | 163 | 1 | 9 |
| α-helix | 167-170 | 4 | |
| β-strand | 181-185 | 5 | 19 |
| α-helix | 188-191 | 4 | |
| α-helix | 194-198 | 5 | |
| α-helix | 200-202 | 3 | |
4 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 |
|---|
| AP-2 complex subunit sigma | D, F, I, L | protein | 142 | Rattus norvegicus | P62744 (AlphaFold model) |
| AP-2 complex subunit alpha-2 | A, B, G, J | protein | 398 | Rattus norvegicus | P18484 (AlphaFold model) |
| Protein Nef | C, E, H, K | protein | 155 | Human immunodeficiency virus 1 | P04601 (AlphaFold model) |
Sequence of entity 1 (D, F, I, L), FASTA
>4NEE_1 AP-2 complex subunit sigma (chains D, F, I, L)
MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYR
RYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLA
GEIRETSQTKVLKQLLMLQSLE
Sequence of entity 2 (A, B, G, J), FASTA
>4NEE_2 AP-2 complex subunit alpha-2 (chains A, B, G, J)
GAMPAVSKGEGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKY
VCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKN
DLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRT
SPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVT
SASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDPAVRGRLTECLETILNKAQEPPKSK
KVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLAS
SEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAM
Sequence of entity 3 (C, E, H, K), FASTA
>4NEE_3 Protein Nef (chains C, E, H, K)
GXXXXXXXXXXXXXEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQD
ILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPV
SLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYF
Primary citation
How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4. Ren, X., Park, S.Y., Bonifacino, J.S. et al. Elife (2014) 3:e01754-e01754. DOI 10.7554/eLife.01754 · PubMed
Other PDB entries of the same protein (UniProt P62744 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9PWB 2.64 Å, Structure of AP-2 bound to the dileucine motif of CCDC32; combined map
- 6OWO 3.2 Å, cryo-EM structure of phosphorylated ap-2 core bound to necap
- 6QH7 3.4 Å, AP2 clathrin adaptor mu2T156-phosphorylated core with two cargo peptides in open+…
- 6OXL 3.5 Å, cryo-EM structure of phosphorylated ap-2 (mu E302K) bound to necap in the presence of ss…
- 6OWT 3.8 Å, Structure of SIVsmm Nef and SMM tetherin bound to the clathrin adaptor AP-2 complex
Browse structure collections
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