HIV-1 TAR loop in complex with Tat:AFF4:P-TEFb. Determined by X-ray diffraction at 3.5 Å resolution. Released 12 Dec 2018.
Explore 6CYT in 3D Show helices and sheets RCSB PDB PDBe
6CYT contains 41 α-helices and 16 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 | 15 | 1 | 1 |
| α-helix | 16-18 | 3 | |
| β-strand | 19-27 | 9 | 1 |
| β-strand | 32-38 | 7 | 1 |
| β-strand | 44-50 | 7 | 1 |
| α-helix | 61-72 | 12 | |
| β-strand | 78 | 1 | 2 |
| β-strand | 81-86 | 6 | 1 |
| β-strand | 99-104 | 6 | 1 |
| β-strand | 108-109 | 2 | 2 |
| α-helix | 110-115 | 6 | |
| α-helix | 123-142 | 20 | |
| β-strand | 145-146 | 2 | 3 |
| α-helix | 152-154 | 3 | |
| β-strand | 155-157 | 3 | 2 |
| β-strand | 163-165 | 3 | 2 |
| α-helix | 168-170 | 3 | |
| β-strand | 172-173 | 2 | 3 |
| α-helix | 192-194 | 3 | |
| α-helix | 197-200 | 4 | |
| α-helix | 209-224 | 16 | |
| α-helix | 234-245 | 12 | |
| α-helix | 256-258 | 3 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-283 | 9 | |
| α-helix | 286-295 | 10 | |
| α-helix | 306-311 | 6 | |
| α-helix | 313-315 | 3 | |
| α-helix | 320-321 | 2 | |
| α-helix | 325-328 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| α-helix | 16-20 | 5 | |
| α-helix | 25-27 | 3 | |
| α-helix | 31-52 | 22 | |
| β-strand | 55 | 1 | 4 |
| α-helix | 56-69 | 14 | |
| α-helix | 80-94 | 15 | |
| α-helix | 101-112 | 12 | |
| α-helix | 117-120 | 4 | |
| α-helix | 124-143 | 20 | |
| α-helix | 153-163 | 11 | |
| α-helix | 168-184 | 17 | |
| α-helix | 187-189 | 3 | |
| α-helix | 193-208 | 16 | |
| β-strand | 210-211 | 2 | 5 |
| α-helix | 221-224 | 4 | |
| α-helix | 231-246 | 16 | |
| α-helix | 252-255 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 36-38 | 3 | |
| β-strand | 39-40 | 2 | 5 |
| α-helix | 47-55 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-12 | 3 | |
| α-helix | 14 | 1 | |
| β-strand | 15 | 1 | 4 |
| α-helix | 28-31 | 4 | |
| α-helix | 35-37 | 3 | |
| α-helix | 38-42 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cyclin-dependent kinase 9 | A | protein | 332 | Homo sapiens | P50750 (AlphaFold model) |
| Cyclin-T1 | B | protein | 264 | Homo sapiens | O60563 (AlphaFold model) |
| AF4/FMR2 family member 4 | C | protein | 36 | Homo sapiens | Q9UHB7 (AlphaFold model) |
| Protein Tat | D | protein | 58 | Human immunodeficiency virus 1 | P04608 (AlphaFold model) |
| RNA (5'-r(p*ap*up*cp*up*gp*ap*gp*cp*cp*up*gp*gp*gp*ap*gp*cp*u)-3') | N | RNA | 20 | Human immunodeficiency virus 1 |
>6CYT_1 Cyclin-dependent kinase 9 (chains A) GHMAKQYDSVECPFCDEVSKYEKLAKIGQGTFGEVFKARHRKTGQKVALKKVLMENEKEG FPITALREIKILQLLKHENVVNLIEICRTKASPYNRCKGSIYLVFDFCEHDLAGLLSNVL VKFTLSEIKRVMQMLLNGLYYIHRNKILHRDMKAANVLITRDGVLKLADFGLARAFSLAK NSQPNRYTNRVVTLWYRPPELLLGERDYGPPIDLWGAGCIMAEMWTRSPIMQGNTEQHQL ALISQLCGSITPEVWPNVDNYELYEKLELVKGQKRKVKDRLKAYVRDPYALDLIDKLLVL DPAQRIDSDDALNHDFFWSDPMPSDLKGMLST
>6CYT_2 Cyclin-T1 (chains B) MEGERKNNNKRWYFTREQLENSPSRRFGVDPDKELSYRQQAANLLQDMGQRLNVSQLTIN TAIVYMHRFYMIQSFTQFPGNSVAPAALFLAAKVEEQPKKLEHVIKVAHTCLHPQESLPD TRSEAYLQQVQDLVILESIILQTLGFELTIDHPHTHVVKCTQLVRASKDLAQTSYFMATN SLHLTTFSLQYTPPVVACVCIHLACKWSNWEIPVSTDGKHWWEYVDATVTLELLDELTHE FLQILEKTPNRLKRIWNWRACEAA
>6CYT_3 AF4/FMR2 family member 4 (chains C) SPLFAEPYKVTSKEDYLSSRIQSMLGNYDEMKDFIG
>6CYT_4 Protein Tat (chains D) XMEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRR
>6CYT_5 RNA (5'-R(P*AP*UP*CP*UP*GP*AP*GP*CP*CP*UP*GP*GP*GP*AP*GP*CP*U)-3') (chains N) GAUCUGAGCCUGGGAGCUCA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural mechanism for HIV-1 TAR loop recognition by Tat and the super elongation complex. Schulze-Gahmen, U., Hurley, J.H. Proc Natl Acad Sci U S A (2018) 115:12973-12978. DOI 10.1073/pnas.1806438115 · PubMed
Other PDB entries of the same protein (UniProt P50750 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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