7U0F: HIV-1 Rev
HIV-1 Rev in complex with tubulin. Determined by electron microscopy at 3.53 Å resolution. Released 23 Aug 2023.
- Method
- Electron microscopy
- Resolution
- 3.53 Å
- Organisms
- Sus scrofa, Human immunodeficiency virus 1
- Chains
- 10
- Atoms
- 16,569
- Mol. weight
- 278.39 kDa
- Released
- 23 Aug 2023
Explore 7U0F in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7U0F contains 87 α-helices and 61 β-strands across 10 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: 21 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-9 | 4 | 1 |
| α-helix | 11-27 | 17 | |
| β-strand | 55 | 1 | 2 |
| β-strand | 61 | 1 | 2 |
| β-strand | 65-68 | 4 | 1 |
| β-strand | 69 | 1 | 3 |
| α-helix | 73-79 | 7 | |
| β-strand | 94 | 1 | 3 |
| α-helix | 104 | 1 | |
| α-helix | 105-109 | 5 | |
| α-helix | 111-113 | 3 | |
| α-helix | 115-126 | 12 | |
| β-strand | 137-140 | 4 | 1 |
| α-helix | 147-160 | 14 | |
| β-strand | 168-172 | 5 | 1 |
| α-helix | 183-193 | 11 | |
| β-strand | 201-205 | 5 | 1 |
| α-helix | 206-214 | 9 | |
| α-helix | 224-243 | 20 | |
| α-helix | 252-259 | 8 | |
| β-strand | 268-271 | 4 | 4 |
| α-helix | 290-293 | 4 | |
| α-helix | 298-300 | 3 | |
| β-strand | 312 | 1 | 5 |
| β-strand | 315 | 1 | 4 |
| β-strand | 318 | 1 | 6 |
| β-strand | 319 | 1 | 7 |
| α-helix | 328-331 | 4 | |
| α-helix | 332-336 | 5 | |
| β-strand | 343 | 1 | 5 |
| β-strand | 355 | 1 | 7 |
| α-helix | 359-363 | 5 | |
| β-strand | 376 | 1 | 6 |
| β-strand | 377-380 | 4 | 4 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 406-408 | 3 | |
| α-helix | 415-431 | 17 | |
| α-helix | 432-436 | 5 | |
Chain B: 18 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4 | 1 | 8 |
| β-strand | 6-8 | 3 | 9 |
| α-helix | 13-24 | 12 | |
| α-helix | 44-48 | 5 | |
| β-strand | 52-53 | 2 | 10 |
| β-strand | 59-60 | 2 | 10 |
| β-strand | 63-65 | 3 | 9 |
| α-helix | 70-76 | 7 | |
| β-strand | 90 | 1 | 9 |
| α-helix | 101-105 | 5 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-124 | 12 | |
| β-strand | 132-137 | 6 | 8 |
| α-helix | 143-158 | 16 | |
| β-strand | 163-168 | 6 | 8 |
| β-strand | 169 | 1 | 11 |
| α-helix | 170-171 | 2 | |
| α-helix | 181-186 | 6 | |
| α-helix | 189-192 | 4 | |
| β-strand | 198-200 | 3 | 8 |
| β-strand | 202 | 1 | 11 |
| α-helix | 205-212 | 8 | |
| α-helix | 222-241 | 20 | |
| α-helix | 250-257 | 8 | |
| β-strand | 265-266 | 2 | 8 |
| β-strand | 269-270 | 2 | 12 |
| α-helix | 287-290 | 4 | |
| β-strand | 315-316 | 2 | 13 |
| α-helix | 324-335 | 12 | |
| β-strand | 351-352 | 2 | 13 |
| β-strand | 366-367 | 2 | 12 |
| α-helix | 373-389 | 17 | |
| α-helix | 395-397 | 3 | |
| α-helix | 406-426 | 21 | |
Chain C: 18 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4 | 1 | |
| β-strand | 5-8 | 4 | 14 |
| α-helix | 10-27 | 18 | |
| β-strand | 66-67 | 2 | 14 |
| α-helix | 72-79 | 8 | |
| α-helix | 103-108 | 6 | |
| α-helix | 115-124 | 10 | |
| β-strand | 135-138 | 4 | 14 |
| α-helix | 147-159 | 13 | |
| β-strand | 168 | 1 | 14 |
| β-strand | 171-172 | 2 | 15 |
| α-helix | 183-190 | 8 | |
| α-helix | 191-195 | 5 | |
| β-strand | 201 | 1 | 14 |
| β-strand | 204-205 | 2 | 15 |
| α-helix | 207-211 | 5 | |
| α-helix | 212-216 | 5 | |
| α-helix | 224-243 | 20 | |
| α-helix | 252-259 | 8 | |
| β-strand | 269 | 1 | 16 |
| α-helix | 290-293 | 4 | |
| β-strand | 312 | 1 | 17 |
| β-strand | 318 | 1 | 18 |
| α-helix | 327-335 | 9 | |
| β-strand | 343 | 1 | 17 |
| α-helix | 361-364 | 4 | |
| β-strand | 376 | 1 | 18 |
| β-strand | 379 | 1 | 16 |
| β-strand | 381 | 1 | 17 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-401 | 17 | |
| α-helix | 415-430 | 16 | |
Chain D: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 19 |
| α-helix | 14-25 | 12 | |
| α-helix | 44-48 | 5 | |
| β-strand | 52-55 | 4 | 20 |
| β-strand | 58-60 | 3 | 20 |
| β-strand | 64-65 | 2 | 19 |
| α-helix | 71-76 | 6 | |
| α-helix | 101-106 | 6 | |
| α-helix | 109-113 | 5 | |
| α-helix | 114-123 | 10 | |
| β-strand | 130-135 | 6 | 19 |
| α-helix | 143-158 | 16 | |
| β-strand | 168-170 | 3 | 21 |
| α-helix | 182-193 | 12 | |
| β-strand | 199 | 1 | 22 |
| β-strand | 201-203 | 3 | 21 |
| α-helix | 205-213 | 9 | |
| α-helix | 222-241 | 20 | |
| α-helix | 250-257 | 8 | |
| β-strand | 265 | 1 | 22 |
| β-strand | 269 | 1 | 23 |
| α-helix | 286-290 | 5 | |
| β-strand | 313-314 | 2 | 24 |
| α-helix | 324-336 | 13 | |
| β-strand | 367 | 1 | 23 |
| β-strand | 368-369 | 2 | 24 |
| α-helix | 375-387 | 13 | |
| α-helix | 405-425 | 21 | |
Chain E: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-24 | 10 | |
| α-helix | 26-28 | 3 | |
| α-helix | 37-61 | 25 | |
Chain F: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-24 | 8 | |
| α-helix | 41-59 | 19 | |
Chain G: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-22 | 10 | |
| α-helix | 35-61 | 27 | |
Chain H: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-24 | 12 | |
| α-helix | 27-29 | 3 | |
| α-helix | 37-61 | 25 | |
2 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 |
|---|
| Tubulin alpha-1A chain | A, C | protein | 451 | Sus scrofa | P02550 (AlphaFold model) |
| Tubulin beta chain | B, D | protein | 445 | Sus scrofa | P02554 (AlphaFold model) |
| Protein Rev | E, F, G, H, I, J | protein | 116 | Human immunodeficiency virus 1 | P04616 |
Sequence of entity 1 (A, C), FASTA
>7U0F_1 Tubulin alpha-1A chain (chains A, C)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Sequence of entity 2 (B, D), FASTA
>7U0F_2 Tubulin beta chain (chains B, D)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA
Sequence of entity 3 (E, F, G, H, I, J), FASTA
>7U0F_3 Protein Rev (chains E, F, G, H, I, J)
MAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERIL
STYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGAKE
Primary citation
Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev. Eren, E., Watts, N.R., Randazzo, D. et al. Structure (2023) 31:1233. DOI 10.1016/j.str.2023.07.009 · PubMed
Other PDB entries of the same protein (UniProt P02550 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7X4N 2.88 Å, Crystal Structure of C. elegans kinesin-4 KLP-12 complexed with tubulin and DARPin
- 9T1D 2.9 Å, Cryo-EM reconstruction of undecorated GDP microtubule
- 6MZG 3.21 Å, Structural Basis of Tubulin Recruitment and Assembly by Microtubule Polymerases with…
- 8QAU 3.54 Å, Outer kinetochore Ndc80-Dam1 alpha/beta-tubulin complex
- 8X9P 3.54 Å, HURP (428-534)-alpha-tubulin-beta-tubulin complex
- 6MZE 3.6 Å, Structural Basis of Tubulin Recruitment and Assembly by Microtubule Polymerases with…
- 6KIQ 3.62 Å, Complex of yeast cytoplasmic dynein MTBD-High and MT with DTT
- 1TUB 3.7 Å, Tubulin alpha-beta dimer, electron diffraction
- 9EDT 3.7 Å, Tubulin cofactors D,E,G bound to tubulin dimer
- 9EEB 3.7 Å, Tubulin cofactors D,E,G bound to tubulin dimer
- 9EDR 3.8 Å, Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin
- 9EDS 3.8 Å, Tubulin cofactors D,E,G,C bound to tubulin dimer -- TBCC N terminus unbound
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