The PDZ domain of MAGI1_2 complexed with the PDZ-binding motif of HPV35-E6. Determined by X-ray diffraction at 2.6 Å resolution. Released 27 Jul 2022.
Explore 7P71 in 3D Show helices and sheets RCSB PDB PDBe
7P71 contains 52 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 |
|---|---|---|---|
| α-helix | 463-465 | 3 | |
| β-strand | 469-476 | 8 | 1 |
| β-strand | 478 | 1 | 2 |
| β-strand | 481 | 1 | 2 |
| β-strand | 484-487 | 4 | 1 |
| β-strand | 497-501 | 5 | 1 |
| α-helix | 506-510 | 5 | |
| β-strand | 518-522 | 5 | 1 |
| β-strand | 526 | 1 | 1 |
| α-helix | 532-541 | 10 | |
| α-helix | 543 | 1 | |
| β-strand | 547-554 | 8 | 1 |
| α-helix | 567-569 | 3 | |
| α-helix | 574-586 | 13 | |
| α-helix | 592-599 | 8 | |
| α-helix | 604-618 | 15 | |
| α-helix | 622-629 | 8 | |
| α-helix | 633-642 | 10 | |
| α-helix | 645-656 | 12 | |
| α-helix | 664-673 | 10 | |
| α-helix | 676-690 | 15 | |
| α-helix | 694-701 | 8 | |
| α-helix | 704-714 | 11 | |
| α-helix | 718-722 | 5 | |
| α-helix | 727-739 | 13 | |
| α-helix | 749-758 | 10 | |
| α-helix | 761-774 | 14 | |
| α-helix | 779-786 | 8 | |
| α-helix | 790-803 | 14 | |
| α-helix | 805-815 | 11 | |
| α-helix | 824-833 | 10 | |
| α-helix | 839-850 | 12 | |
| α-helix | 854-861 | 8 | |
| α-helix | 864-874 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 463-465 | 3 | |
| β-strand | 469-476 | 8 | 3 |
| β-strand | 484-487 | 4 | 3 |
| β-strand | 497-501 | 5 | 3 |
| α-helix | 506-510 | 5 | |
| α-helix | 517 | 1 | |
| β-strand | 518-522 | 5 | 3 |
| β-strand | 525-526 | 2 | 3 |
| α-helix | 532-541 | 10 | |
| α-helix | 543 | 1 | |
| β-strand | 547-554 | 8 | 3 |
| α-helix | 574-586 | 13 | |
| α-helix | 592-599 | 8 | |
| α-helix | 604-618 | 15 | |
| α-helix | 622-627 | 6 | |
| α-helix | 632-642 | 11 | |
| α-helix | 645-655 | 11 | |
| α-helix | 664-673 | 10 | |
| α-helix | 676-690 | 15 | |
| α-helix | 694-701 | 8 | |
| α-helix | 704-714 | 11 | |
| α-helix | 718-720 | 3 | |
| α-helix | 727-738 | 12 | |
| α-helix | 739-743 | 5 | |
| α-helix | 749-758 | 10 | |
| α-helix | 761-774 | 14 | |
| α-helix | 779-786 | 8 | |
| α-helix | 790-816 | 27 | |
| α-helix | 824-833 | 10 | |
| α-helix | 839-850 | 12 | |
| α-helix | 854-861 | 8 | |
| α-helix | 865-874 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 146-148 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 147-148 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1,Annexin A2 | A, B | protein | 427 | Homo sapiens | P07355 (AlphaFold model), Q96QZ7 (AlphaFold model) |
| Protein E6 | C, D | protein | 13 | Human papillomavirus 35 | P27228 (AlphaFold model) |
>7P71_1 Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1,Annexin A2 (chains A, B) GSMGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDG KMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLGSSAYGSVKAYTN FDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALS GHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYK TDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPK WISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFAD RLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALL YLCGGDD
>7P71_2 Protein E6 (chains C, D) TDDSKPTRRETEV
Water and common crystallization additives (GOL) are not listed.
Quantitative fragmentomics allow affinity mapping of interactomes. Gogl, G., Zambo, B., Kostmann, C. et al. Nat Commun (2022) 13:5472-5472. DOI 10.1038/s41467-022-33018-0 · PubMed
Other PDB entries of the same protein (UniProt P07355 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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