Human ARTD2 in complex with DNA oligonucleotides. Determined by X-ray diffraction at 2.8 Å resolution. Released 19 May 2021.
Explore 7AEO in 3D Show helices and sheets RCSB PDB PDBe
7AEO contains 25 α-helices and 29 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 | 92-94 | 3 | |
| β-strand | 105-107 | 3 | 1 |
| β-strand | 109-110 | 2 | 2 |
| β-strand | 113-114 | 2 | 2 |
| β-strand | 116-123 | 8 | 1 |
| α-helix | 124-126 | 3 | |
| β-strand | 128-139 | 12 | 1 |
| β-strand | 145-153 | 9 | 1 |
| β-strand | 159-166 | 8 | 1 |
| α-helix | 169-184 | 16 | |
| α-helix | 196-197 | 2 | |
| α-helix | 201 | 1 | |
| β-strand | 202-204 | 3 | 1 |
| β-strand | 206 | 1 | 3 |
| α-helix | 236-245 | 10 | |
| α-helix | 248-259 | 12 | |
| α-helix | 262-264 | 3 | |
| α-helix | 269 | 1 | |
| β-strand | 270 | 1 | 3 |
| α-helix | 271 | 1 | |
| α-helix | 272-290 | 19 | |
| α-helix | 297-308 | 12 | |
| β-strand | 313 | 1 | 4 |
| β-strand | 315 | 1 | 4 |
| α-helix | 317-320 | 4 | |
| α-helix | 324-335 | 12 | |
| α-helix | 357-365 | 9 | |
| β-strand | 367-368 | 2 | 5 |
| β-strand | 371 | 1 | 6 |
| α-helix | 377-388 | 12 | |
| β-strand | 397-406 | 10 | 6 |
| β-strand | 408-409 | 2 | 5 |
| α-helix | 412-415 | 4 | |
| β-strand | 423-429 | 7 | 6 |
| α-helix | 432-434 | 3 | |
| α-helix | 435-441 | 7 | |
| β-strand | 461-463 | 3 | 7 |
| β-strand | 464 | 1 | 6 |
| α-helix | 467-471 | 5 | |
| α-helix | 472-474 | 3 | |
| β-strand | 484-491 | 8 | 6 |
| β-strand | 495-498 | 4 | 7 |
| α-helix | 505-509 | 5 | |
| β-strand | 514-517 | 4 | 7 |
| β-strand | 519-523 | 5 | 8 |
| α-helix | 525-527 | 3 | |
| β-strand | 529-531 | 3 | 6 |
| β-strand | 534-536 | 3 | 6 |
| β-strand | 541-543 | 3 | 8 |
| α-helix | 552-553 | 2 | |
| β-strand | 554-556 | 3 | 8 |
| β-strand | 558-561 | 4 | 7 |
| α-helix | 564-566 | 3 | |
| β-strand | 567-579 | 13 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Poly [ADP-ribose] polymerase 2 | A | protein | 496 | Homo sapiens | Q9UGN5 (AlphaFold model) |
| DNA | B | DNA | 16 | synthetic construct | |
| DNA | C | DNA | 16 | synthetic construct |
>7AEO_1 Poly [ADP-ribose] polymerase 2 (chains A) SMGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSV WMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMD YATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPL GKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKEL SEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQ STHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAP PEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEG LLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQV RMRYLLKVQFNFLQLW
>7AEO_2 DNA (chains B) TGTGCTCCGGGTCGTC
>7AEO_3 DNA (chains C) GACGACCCGGAGCACA
Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition. Obaji, E., Maksimainen, M.M., Galera-Prat, A. et al. Nat Commun (2021) 12:3479-3479. DOI 10.1038/s41467-021-23800-x · PubMed
Other PDB entries of the same protein (UniProt Q9UGN5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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