Crystal structure of the Prototype Foamy Virus (PFV) intasome in complex with magnesium and the INSTI L-870,810. Determined by X-ray diffraction at 2.51 Å resolution. Released 17 Nov 2010.
Explore 3OYF in 3D Show helices and sheets RCSB PDB PDBe
3OYF contains 38 α-helices and 29 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 9-16 | 8 | |
| β-strand | 30-33 | 4 | 1 |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 44-47 | 4 | 1 |
| α-helix | 51-65 | 15 | |
| α-helix | 69-76 | 8 | |
| β-strand | 80 | 1 | 1 |
| α-helix | 85-93 | 9 | |
| α-helix | 97-102 | 6 | |
| α-helix | 104-105 | 2 | |
| β-strand | 108-109 | 2 | 2 |
| α-helix | 110-113 | 4 | |
| α-helix | 115-117 | 3 | |
| β-strand | 124-130 | 7 | 3 |
| β-strand | 136 | 1 | 4 |
| β-strand | 139 | 1 | 4 |
| β-strand | 141-147 | 7 | 3 |
| β-strand | 153-158 | 6 | 3 |
| α-helix | 163-174 | 12 | |
| β-strand | 181-184 | 4 | 3 |
| α-helix | 188-191 | 4 | |
| α-helix | 193-200 | 8 | |
| α-helix | 204 | 1 | |
| β-strand | 205-208 | 4 | 3 |
| α-helix | 209-210 | 2 | |
| α-helix | 214-217 | 4 | |
| α-helix | 218-235 | 18 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-254 | 9 | |
| β-strand | 258 | 1 | 5 |
| β-strand | 263 | 1 | 5 |
| α-helix | 265-270 | 6 | |
| α-helix | 288-300 | 13 | |
| α-helix | 308-311 | 4 | |
| β-strand | 314-315 | 2 | 2 |
| β-strand | 322-325 | 4 | 6 |
| β-strand | 326 | 1 | 7 |
| α-helix | 327 | 1 | |
| α-helix | 330-331 | 2 | |
| β-strand | 337 | 1 | 7 |
| α-helix | 338-340 | 3 | |
| β-strand | 341-348 | 8 | 6 |
| β-strand | 351-355 | 5 | 6 |
| β-strand | 361-365 | 5 | 6 |
| α-helix | 366-368 | 3 | |
| β-strand | 369-371 | 3 | 6 |
| α-helix | 372 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 117-119 | 3 | |
| β-strand | 124-130 | 7 | 8 |
| β-strand | 136 | 1 | 9 |
| β-strand | 139 | 1 | 9 |
| β-strand | 141-147 | 7 | 8 |
| β-strand | 153-158 | 6 | 8 |
| α-helix | 163-173 | 11 | |
| β-strand | 181-184 | 4 | 8 |
| α-helix | 188-191 | 4 | |
| α-helix | 193-201 | 9 | |
| α-helix | 204 | 1 | |
| β-strand | 205-208 | 4 | 8 |
| α-helix | 209-210 | 2 | |
| α-helix | 218-235 | 18 | |
| α-helix | 243-245 | 3 | |
| α-helix | 246-254 | 9 | |
| α-helix | 257-258 | 2 | |
| α-helix | 265-270 | 6 | |
| α-helix | 286-287 | 2 | |
| α-helix | 288-297 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PFV integrase | A, B | protein | 395 | Human spumaretrovirus | P14350 |
| DNA (5'-d(*ap*tp*tp*gp*tp*cp*ap*tp*gp*gp*ap*ap*tp*tp*tp*cp*gp*cp*a)-3') | C | DNA | 19 | ||
| DNA (5'-d(*tp*gp*cp*gp*ap*ap*ap*tp*tp*cp*cp*ap*tp*gp*ap*cp*a)-3') | D | DNA | 17 |
>3OYF_1 PFV integrase (chains A, B) GPGCNTKKPNLDAELDQLLQGHYIKGYPKQYTYFLEDGKVKVSRPEGVKIIPPQSDRQKI VLQAHNLAHTGREATLLKIANLYWWPNMRKDVVKQLGRCQQCLITNASNKASGPILRPDR PQKPFDKFFIDYIGPLPPSQGYLYVLVVVDGMTGFTWLYPTKAPSTSATVKSLNVLTSIA IPKVIHSDQGAAFTSSTFAEWAKERGIHLEFSTPYHPQSSGKVERKNSDIKRLLTKLLVG RPTKWYDLLPVVQLALNNTYSPVLKYTPHQLLFGIDSNTPFANQDTLDLTREEELSLLQE IRTSLYHPSTPPASSRSWSPVVGQLVQERVARPASLRPRWHKPSTVLKVLNPRTVVILDH LGNNRTVSIDNLKPTSHQNGTTNDTATMDHLEKNE
>3OYF_2 DNA (5'-D(*AP*TP*TP*GP*TP*CP*AP*TP*GP*GP*AP*AP*TP*TP*TP*CP*GP*CP*A)-3') (chains C) ATTGTCATGGAATTTCGCA
>3OYF_3 DNA (5'-D(*TP*GP*CP*GP*AP*AP*AP*TP*TP*CP*CP*AP*TP*GP*AP*CP*A)-3') (chains D) TGCGAAATTCCATGACA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
| MG | Magnesium ion | Mg | 3 |
| ZYP | 5-(1,1-dioxido-1,2-thiazinan-2-yl)-N-(4-fluorobenzyl)-8-hydroxy-1,6-naphthyridi… | C20 H19 F N4 O4 S | 1 |
Water and common crystallization additives (SO4, GOL, NH4) are not listed.
Molecular mechanisms of retroviral integrase inhibition and the evolution of viral resistance. Hare, S., Vos, A.M., Clayton, R.F. et al. Proc Natl Acad Sci U S A (2010) 107:20057-20062. DOI 10.1073/pnas.1010246107 · PubMed
Other PDB entries of the same protein (UniProt P14350), best resolution first:
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