6CRI: PDB entry 6CRI
Structure of the cargo bound AP-1:Arf1:tetherin-Nef stable closed trimer. Determined by electron microscopy at 6.8 Å resolution. Released 1 Aug 2018.
- Method
- Electron microscopy
- Resolution
- 6.8 Å
- Organisms
- Homo sapiens, Human immunodeficiency virus 1, Mus musculus
- Chains
- 24
- Atoms
- 53,049
- Mol. weight
- 885.69 kDa
- Ligands
- GTP, MG
- Released
- 1 Aug 2018
Explore 6CRI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6CRI contains 357 α-helices and 203 β-strands across 24 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: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-8 | 5 | 32 |
| β-strand | 14-19 | 6 | 32 |
| α-helix | 25-40 | 16 | |
| β-strand | 49-52 | 4 | 32 |
| β-strand | 55-59 | 5 | 32 |
| β-strand | 66-71 | 6 | 32 |
| α-helix | 78-94 | 17 | |
| β-strand | 99 | 1 | 33 |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 34 |
| β-strand | 122-123 | 2 | 34 |
| α-helix | 129-141 | 13 | |
Chains b and S: 5 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-8 | 5 | 51 |
| β-strand | 14-19 | 6 | 51 |
| α-helix | 25-40 | 16 | |
| β-strand | 49-52 | 4 | 51 |
| β-strand | 55-59 | 5 | 51 |
| β-strand | 66-71 | 6 | 51 |
| α-helix | 78-94 | 17 | |
| α-helix | 100-105 | 6 | |
| α-helix | 107-117 | 11 | |
| β-strand | 118-119 | 2 | 52 |
| β-strand | 122-123 | 2 | 52 |
| α-helix | 129-141 | 13 | |
Chains B, I and J: 42 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-22 | 8 | |
| α-helix | 27-42 | 16 | |
| α-helix | 48-50 | 3 | |
| α-helix | 51-56 | 6 | |
| α-helix | 63-75 | 13 | |
| α-helix | 83-85 | 3 | |
| α-helix | 88-94 | 7 | |
| α-helix | 100-112 | 13 | |
| α-helix | 123-130 | 8 | |
| α-helix | 135-151 | 17 | |
| α-helix | 153-159 | 7 | |
| α-helix | 161-169 | 9 | |
| α-helix | 174-190 | 17 | |
| α-helix | 201-211 | 11 | |
| α-helix | 216-225 | 10 | |
| α-helix | 234-244 | 11 | |
| α-helix | 245-249 | 5 | |
| β-strand | 250 | 1 | 1 |
| α-helix | 253-266 | 14 | |
| α-helix | 275-282 | 8 | |
| α-helix | 285-290 | 6 | |
| α-helix | 291-293 | 3 | |
| α-helix | 296-312 | 17 | |
| α-helix | 322-324 | 3 | |
| α-helix | 332-344 | 13 | |
| α-helix | 348-350 | 3 | |
| α-helix | 351-359 | 9 | |
| α-helix | 367-383 | 17 | |
| α-helix | 388-399 | 12 | |
| α-helix | 404-420 | 17 | |
| α-helix | 429-432 | 4 | |
| α-helix | 442-454 | 13 | |
| α-helix | 462-469 | 8 | |
| α-helix | 473-475 | 3 | |
| α-helix | 479-494 | 16 | |
| α-helix | 500-507 | 8 | |
| α-helix | 508-512 | 5 | |
| α-helix | 517-532 | 16 | |
| α-helix | 534-540 | 7 | |
| α-helix | 547-550 | 4 | |
| α-helix | 554-556 | 3 | |
| α-helix | 557-564 | 8 | |
| β-strand | 569 | 1 | 2 |
| α-helix | 570-574 | 5 | |
Chains c, d and T: 1 helix, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9 | 1 | 19 |
| α-helix | 10-12 | 3 | |
Chain C: 6 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 19-22 | 4 | 3 |
| β-strand | 23 | 1 | 4 |
| α-helix | 30-38 | 9 | |
| β-strand | 51-58 | 8 | 3 |
| β-strand | 61-68 | 8 | 3 |
| α-helix | 72-74 | 3 | |
| α-helix | 76-78 | 3 | |
| β-strand | 90-91 | 2 | 4 |
| α-helix | 97-110 | 14 | |
| β-strand | 123-125 | 3 | 4 |
| α-helix | 138-143 | 6 | |
| β-strand | 155-157 | 3 | 4 |
| β-strand | 159 | 1 | 5 |
| β-strand | 164 | 1 | 5 |
| α-helix | 166-177 | 12 | |
Chains G, Q and R: 41 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-15 | 9 | |
| α-helix | 20-39 | 20 | |
| α-helix | 46-58 | 13 | |
| α-helix | 64-66 | 3 | |
| α-helix | 67-74 | 8 | |
| α-helix | 79-92 | 14 | |
| α-helix | 95-97 | 3 | |
| α-helix | 100-102 | 3 | |
| α-helix | 103-110 | 8 | |
| α-helix | 116-129 | 14 | |
| α-helix | 132-137 | 6 | |
| α-helix | 139-144 | 6 | |
| α-helix | 151-167 | 17 | |
| α-helix | 169-174 | 6 | |
| α-helix | 188-204 | 17 | |
| α-helix | 206-208 | 3 | |
| α-helix | 209-212 | 4 | |
| α-helix | 216-228 | 13 | |
| β-strand | 236-237 | 2 | 6 |
| β-strand | 240-241 | 2 | 6 |
| α-helix | 243-255 | 13 | |
| α-helix | 262-266 | 5 | |
| α-helix | 268-274 | 7 | |
| α-helix | 283-298 | 16 | |
| α-helix | 303-318 | 16 | |
| α-helix | 322-334 | 13 | |
| α-helix | 340-344 | 5 | |
| α-helix | 347-354 | 8 | |
| α-helix | 359-372 | 14 | |
| α-helix | 378-390 | 13 | |
| α-helix | 394-411 | 18 | |
| α-helix | 416-428 | 13 | |
| α-helix | 437-447 | 11 | |
| α-helix | 453-463 | 11 | |
| α-helix | 470-482 | 13 | |
| α-helix | 484-487 | 4 | |
| α-helix | 504-514 | 11 | |
| α-helix | 522-532 | 11 | |
| α-helix | 544-550 | 7 | |
| α-helix | 551-553 | 3 | |
| α-helix | 557-571 | 15 | |
| α-helix | 578-580 | 3 | |
| α-helix | 582-585 | 4 | |
Chains H, U and V: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-24 | 7 | 7 |
| α-helix | 30-37 | 8 | |
| β-strand | 51-58 | 8 | 7 |
| β-strand | 61-68 | 8 | 7 |
| α-helix | 75-81 | 7 | |
| β-strand | 87-93 | 7 | 7 |
| α-helix | 100-111 | 12 | |
| β-strand | 120-126 | 7 | 7 |
| α-helix | 136-143 | 8 | |
| α-helix | 145-147 | 3 | |
| β-strand | 153-156 | 4 | 7 |
| β-strand | 159 | 1 | 8 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 8 |
| α-helix | 166-175 | 10 | |
Chain K: 6 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 19-22 | 4 | 21 |
| β-strand | 23-24 | 2 | 22 |
| α-helix | 30-38 | 9 | |
| β-strand | 51-58 | 8 | 21 |
| β-strand | 61-68 | 8 | 21 |
| α-helix | 72-74 | 3 | |
| α-helix | 76-78 | 3 | |
| β-strand | 90-91 | 2 | 22 |
| α-helix | 97-110 | 14 | |
| β-strand | 123-125 | 3 | 22 |
| α-helix | 138-143 | 6 | |
| β-strand | 155-157 | 3 | 22 |
| α-helix | 166-177 | 12 | |
6 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 |
|---|
| Bone marrow stromal antigen 2, Protein Nef chimera | N, T, Y, Z, c, d | protein | 264 | Homo sapiens, Human immunodeficiency virus 1 | P03404, Q10589 (AlphaFold model) |
| AP-1 complex subunit beta-1 | B, I, J | protein | 570 | Homo sapiens | Q10567 (AlphaFold model) |
| ADP-ribosylation factor 1 | C, H, K, L, U, V | protein | 165 | Homo sapiens | P84077 (AlphaFold model) |
| AP-1 complex subunit gamma-1 | G, Q, R | protein | 585 | Mus musculus | P22892 |
| AP-1 complex subunit mu-1 | M, W, X | protein | 422 | Mus musculus | P35585 |
| AP-1 complex subunit sigma-3 | S, a, b | protein | 142 | Homo sapiens | Q96PC3 |
Sequence of entity 1 (N, T, Y, Z, c, d), FASTA
>6CRI_1 Bone marrow stromal antigen 2, Protein Nef chimera (chains N, T, Y, Z, c, d)
MSYYHHHHHHDYDIPTTENLYFQGAMGSASTSYDYCRVPMEDGDKRCKGSDEASEGSGMG
GKWSKSSVIGWPAVRERMRRAEPAADGVGAVSRDLEKHGAITSSNTAANNAACAWLEAQE
EEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFP
DWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLE
WRFDSRLAFHHVARELHPEYFKNC
Sequence of entity 2 (B, I, J), FASTA
>6CRI_2 AP-1 complex subunit beta-1 (chains B, I, J)
EIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYL
MNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDE
DPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANAVAALSEIAESHPS
SNLLDLNPQSINKLLTALNECTEWGQIFILDCLANYMPKDDREAQSICERVTPRLSHANS
AVVLSAVKVLMKFMEMLSKDLDYYGTLLKKLAPPLVTLLSAEPELQYVALRNINLIVQKR
PEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELREYATEVDVDFVRKA
VRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLC
ENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLEGFHDKSTQVQLQLLTAIVKLFL
KKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETD
LIEPTLLDELICYIGTLASVYHKPPSAFVE
Sequence of entity 3 (C, H, K, L, U, V), FASTA
>6CRI_3 ADP-ribosylation factor 1 (chains C, H, K, L, U, V)
EMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGLDKIRP
LWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNA
AEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
Sequence of entity 4 (G, Q, R), FASTA
>6CRI_4 AP-1 complex subunit gamma-1 (chains G, Q, R)
PIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPA
HFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLAL
CTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLL
NEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDP
FLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSES
GLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKR
RAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIM
RVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEY
GDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNR
IKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVME
Sequence of entity 5 (M, W, X), FASTA
>6CRI_5 AP-1 complex subunit mu-1 (chains M, W, X)
SASAVYVLDLKGKVLICRNYRGDVDMSEVEHFMPILMEKEEEGMLSPILAHGGVRFMWIK
HNNLYLVATSKKNACVSLVFSFLYKVVQVFSEYFKELEEESIRDNFVIIYELLDELMDFG
YPQTTDSKILQEYITQEGHKLETGAPRPPATVTNAVSWRSEGIKYRKNEVFLDVIEAVNL
LVSANGNVLRSEIVGSIKMRVFLSGMPELRLGLNDKVLFDNTGRGKSKSVELEDVKFHQC
VRLSRFENDRTISFIPPDGEFELMSYRLNTHVKPLIWIESVIEKHSHSRIEYMVKAKSQF
KRRSTANNVEIHIPVPNDADSPKFKTTVGSVKWVPENSEIVWSVKSFPGGKEYLMRAHFG
LPSVEAEDKEGKPPISVKFEIPYFTTSGIQVRYLKIIEKSGYQALPWVRYITQNGDYQLR
TQ
Sequence of entity 6 (S, a, b), FASTA
>6CRI_6 AP-1 complex subunit sigma-3 (chains S, a, b)
MIHFILLFSRQGKLRLQKWYITLPDKERKKITREIVQIILSRGHRTSSFVDWKELKLVYK
RYASLYFCCAIENQDNELLTLEIVHRYVELLDKYFGNVCELDIIFNFEKAYFILDEFIIG
GEIQETSKKIAVKAIEDSDMLQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 6 |
| MG | Magnesium ion | Mg | 6 |
Primary citation
HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation. Morris, K.L., Buffalo, C.Z., Sturzel, C.M. et al. Cell (2018) 174:659-671.e14. DOI 10.1016/j.cell.2018.07.004 · PubMed
Other PDB entries of the same protein (UniProt P03404), best resolution first:
- 3TB8 3.71 Å, Crystal structure of full-length myristoylated HIV-1 Nef
- 1ZEC NMR Solution structure of NEF1-25, 20 structures
Browse structure collections
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