Human topoisomerase I (Topo70) double mutant K532R/Y723F. Determined by X-ray diffraction at 3.13 Å resolution. Released 16 Dec 2003.
Explore 1R49 in 3D Show helices and sheets RCSB PDB PDBe
1R49 contains 28 α-helices and 23 β-strands across 1 chain. 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 | 211-212 | 2 | |
| β-strand | 220-221 | 2 | 1 |
| β-strand | 226 | 1 | 2 |
| α-helix | 227-235 | 9 | |
| β-strand | 240-242 | 3 | 3 |
| β-strand | 245-247 | 3 | 3 |
| α-helix | 251-262 | 12 | |
| α-helix | 268-270 | 3 | |
| α-helix | 272-284 | 13 | |
| α-helix | 288-293 | 6 | |
| β-strand | 300-301 | 2 | 3 |
| α-helix | 303-317 | 15 | |
| α-helix | 321-338 | 18 | |
| β-strand | 340-343 | 4 | 1 |
| β-strand | 346-349 | 4 | 1 |
| β-strand | 350 | 1 | 4 |
| β-strand | 354 | 1 | 2 |
| α-helix | 355-358 | 4 | |
| β-strand | 359-360 | 2 | 5 |
| β-strand | 373-374 | 2 | 5 |
| α-helix | 375-378 | 4 | |
| β-strand | 383-385 | 3 | 6 |
| α-helix | 392-395 | 4 | |
| β-strand | 403-405 | 3 | 6 |
| β-strand | 414-417 | 4 | 6 |
| α-helix | 423 | 1 | |
| β-strand | 424-427 | 4 | 6 |
| β-strand | 429 | 1 | 4 |
| α-helix | 434-461 | 28 | |
| α-helix | 464-466 | 3 | |
| α-helix | 470-484 | 15 | |
| α-helix | 491-494 | 4 | |
| β-strand | 495 | 1 | 7 |
| β-strand | 498 | 1 | 7 |
| β-strand | 508 | 1 | 8 |
| α-helix | 509-511 | 3 | |
| β-strand | 512-515 | 4 | 9 |
| β-strand | 524-530 | 7 | 9 |
| β-strand | 536-542 | 7 | 9 |
| α-helix | 545-553 | 9 | |
| β-strand | 563 | 1 | 8 |
| α-helix | 570-580 | 11 | |
| α-helix | 588-603 | 16 | |
| α-helix | 612-626 | 15 | |
| α-helix | 648-659 | 12 | |
| α-helix | 662-674 | 13 | |
| α-helix | 679-710 | 32 | |
| α-helix | 726-735 | 10 | |
| α-helix | 740-742 | 3 | |
| α-helix | 746-751 | 6 | |
| α-helix | 753-757 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 5'-d(*ap*ap*ap*ap*ap*gp*ap*cp*tp*tp*ap*gp*ap*ap*ap*ap*ap*tp*tp*tp*tp*t)-3' | B | DNA | 22 | ||
| 5'-d(p*ap*ap*ap*ap*ap*tp*tp*tp*tp*tp*cp*tp*ap*ap*gp*tp*cp*tp*tp*tp*tp*t)-3' | C | DNA | 22 | ||
| DNA topoisomerase I | A | protein | 592 | Homo sapiens | P11387 (AlphaFold model) |
>1R49_1 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*TP*AP*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3' (chains B) AAAAAGACTTAGAAAAATTTTT
>1R49_2 5'-D(P*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*TP*AP*AP*GP*TP*CP*TP*TP*TP*TP*T)-3' (chains C) AAAAATTTTTCTAAGTCTTTTT
>1R49_3 DNA topoisomerase I (chains A) KKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEP LPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNI ITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANF KIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWL VSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVR QRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGRD SIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYN ASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDA KKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQ IALGTSKLNFLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF
The role of lysine 532 in the catalytic mechanism of human topoisomerase I. Interthal, H., Quigley, P.M., Hol, W.G. et al. J Biol Chem (2004) 279:2984-2992. DOI 10.1074/jbc.M309959200 · PubMed
Other PDB entries of the same protein (UniProt P11387 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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