Human DNA Topoisomerase I (70 Kda) In Complex With The Indenoisoquinoline MJ-II-38 and Covalent Complex With A 22 Base Pair DNA Duplex. Determined by X-ray diffraction at 3.0 Å resolution. Released 19 Apr 2005.
Explore 1SC7 in 3D Show helices and sheets RCSB PDB PDBe
1SC7 contains 33 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 | 209-212 | 4 | |
| β-strand | 220-222 | 3 | 1 |
| β-strand | 226 | 1 | 2 |
| α-helix | 227-231 | 5 | |
| β-strand | 240-242 | 3 | 3 |
| β-strand | 245-247 | 3 | 3 |
| α-helix | 251-263 | 13 | |
| α-helix | 268-270 | 3 | |
| α-helix | 272-284 | 13 | |
| α-helix | 288-293 | 6 | |
| α-helix | 297-299 | 3 | |
| β-strand | 300-301 | 2 | 3 |
| α-helix | 305-314 | 10 | |
| α-helix | 321-324 | 4 | |
| α-helix | 327-337 | 11 | |
| 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 | 360 | 1 | 5 |
| β-strand | 373 | 1 | 5 |
| α-helix | 376-378 | 3 | |
| α-helix | 379-381 | 3 | |
| 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 | 434-451 | 18 | |
| α-helix | 454-463 | 10 | |
| α-helix | 470-484 | 15 | |
| β-strand | 495 | 1 | 7 |
| β-strand | 498 | 1 | 7 |
| β-strand | 508 | 1 | 8 |
| β-strand | 512-515 | 4 | 9 |
| β-strand | 524-530 | 7 | 9 |
| α-helix | 532-534 | 3 | |
| β-strand | 536-542 | 7 | 9 |
| α-helix | 545-555 | 11 | |
| β-strand | 563 | 1 | 8 |
| α-helix | 570-578 | 9 | |
| α-helix | 588-604 | 17 | |
| α-helix | 612-625 | 14 | |
| α-helix | 648-650 | 3 | |
| α-helix | 652-674 | 23 | |
| α-helix | 682-686 | 5 | |
| α-helix | 689-701 | 13 | |
| α-helix | 703-709 | 7 | |
| α-helix | 717-722 | 6 | |
| α-helix | 726-733 | 8 | |
| 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*t)-3' | B | DNA | 10 | ||
| 5'-d(*(tgp)p*gp*ap*ap*ap*ap*ap*tp*tp*tp*tp*t)-3' | C | DNA | 12 | ||
| 5'-d(*ap*ap*ap*ap*ap*tp*tp*tp*tp*tp*cp*cp*ap*ap*gp*tp*cp*tp*tp*tp*tp*t)-3' | D | DNA | 22 | ||
| DNA topoisomerase I | A | protein | 592 | Homo sapiens | P11387 (AlphaFold model) |
>1SC7_1 5'-D(*AP*AP*AP*AP*AP*GP*AP*CP*TP*T)-3' (chains B) AAAAAGACTT
>1SC7_2 5'-D(*(TGP)P*GP*AP*AP*AP*AP*AP*TP*TP*TP*TP*T)-3' (chains C) GGAAAAATTTTT
>1SC7_3 5'-D(*AP*AP*AP*AP*AP*TP*TP*TP*TP*TP*CP*CP*AP*AP*GP*TP*CP*TP*TP*TP*TP*T)-3' (chains D) AAAAATTTTTCCAAGTCTTTTT
>1SC7_4 DNA topoisomerase I (chains A) KKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEP LPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNI ITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANF KIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWL VSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVR QRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKD SIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYN ASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDA KKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQ IALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF
| ID | Name | Formula | Copies |
|---|---|---|---|
| M38 | 4-(5,11-dioxo-5H-INDENO[1,2-c]isoquinolin-6(11H)-yl)butanoate | C20 H15 N O4 | 1 |
Water and common crystallization additives (PG4) are not listed.
Structures of three classes of anticancer agents bound to the human topoisomerase I-DNA covalent complex. Staker, B.L., Feese, M.D., Cushman, M. et al. J Med Chem (2005) 48:2336-2345. DOI 10.1021/jm049146p · 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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