Co-crystal structure of maltose binding protein (MBP)-human SENP3 fusion protein in complex with PELP1 peptide. Determined by X-ray diffraction at 2.93 Å resolution. Released 6 Aug 2025.
Explore 9ME8 in 3D Show helices and sheets RCSB PDB PDBe
9ME8 contains 41 α-helices and 35 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 | 2-3 | 2 | |
| β-strand | 7-10 | 4 | 1 |
| α-helix | 17-31 | 15 | |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 43-51 | 9 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 67-72 | 6 | |
| β-strand | 76 | 1 | 2 |
| α-helix | 77-79 | 3 | |
| α-helix | 83-87 | 5 | |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-96 | 6 | |
| β-strand | 98-99 | 2 | 4 |
| β-strand | 102-103 | 2 | 4 |
| β-strand | 105-111 | 7 | 1 |
| β-strand | 114-118 | 5 | 5 |
| β-strand | 128 | 1 | 6 |
| α-helix | 129-131 | 3 | |
| α-helix | 132-142 | 11 | |
| β-strand | 145-147 | 3 | 5 |
| α-helix | 154-163 | 10 | |
| β-strand | 167-172 | 6 | 7 |
| β-strand | 175-182 | 8 | 7 |
| α-helix | 186-200 | 15 | |
| α-helix | 210-218 | 9 | |
| β-strand | 222-227 | 6 | 5 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-236 | 5 | |
| β-strand | 242-245 | 4 | 5 |
| α-helix | 246-248 | 3 | |
| β-strand | 249-250 | 2 | 6 |
| β-strand | 253-254 | 2 | 6 |
| α-helix | 257 | 1 | |
| β-strand | 258-259 | 2 | 8 |
| β-strand | 260-266 | 7 | 1 |
| β-strand | 267 | 1 | 2 |
| α-helix | 273-279 | 7 | |
| α-helix | 280-284 | 5 | |
| α-helix | 287-296 | 10 | |
| β-strand | 301-302 | 2 | 1 |
| β-strand | 304 | 1 | 3 |
| α-helix | 305-311 | 7 | |
| α-helix | 315-326 | 12 | |
| β-strand | 328-329 | 2 | 8 |
| α-helix | 330-331 | 2 | |
| α-helix | 335-351 | 17 | |
| α-helix | 357-368 | 12 | |
| α-helix | 1312-1328 | 17 | |
| β-strand | 1330 | 1 | 9 |
| α-helix | 1336-1347 | 12 | |
| α-helix | 1354-1369 | 16 | |
| β-strand | 1375 | 1 | 9 |
| β-strand | 1380-1383 | 4 | 10 |
| β-strand | 1386-1389 | 4 | 10 |
| α-helix | 1390-1393 | 4 | |
| α-helix | 1394-1396 | 3 | |
| α-helix | 1400-1402 | 3 | |
| α-helix | 1404-1417 | 14 | |
| β-strand | 1422-1424 | 3 | 11 |
| α-helix | 1428-1436 | 9 | |
| α-helix | 1437-1440 | 4 | |
| α-helix | 1450-1452 | 3 | |
| β-strand | 1455-1462 | 8 | 11 |
| β-strand | 1465-1472 | 8 | 11 |
| β-strand | 1477-1481 | 5 | 11 |
| β-strand | 1486-1488 | 3 | 12 |
| α-helix | 1490-1505 | 16 | |
| α-helix | 1509-1511 | 3 | |
| β-strand | 1516-1519 | 4 | 11 |
| α-helix | 1532-1545 | 14 | |
| α-helix | 1553-1555 | 3 | |
| α-helix | 1556-1569 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 765-767 | 3 | 12 |
| α-helix | 775 | 1 | |
| β-strand | 776-778 | 3 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose/maltodextrin-binding periplasmic protein,Sentrin-specific protease 3 | A | protein | 635 | Homo sapiens | Q9H4L4 (AlphaFold model) |
| Proline-, glutamic acid- and leucine-rich protein 1 | B | protein | 18 | Homo sapiens | Q8IZL8 (AlphaFold model) |
>9ME8_1 Maltose/maltodextrin-binding periplasmic protein,Sentrin-specific protease 3 (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSK VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNAAAEEHVTCVQSILDEFLQTYGSLIPLSTDEVVEKLEDIFQQEFSTPSRKGL VLQLIQSYQRMPGNAMVRGFRVAYKRHVLTMDDLGTLYGQNWLNDQVMNMYGDLVMDTVP EKVHFFNSFFYDKLRTKGYDGVKRWTKNVDIFNKELLLIPIHLEVHWSLISVDVRRRTIT YFDSQRTLNRRCPKHIAKYLQAEAVKKDRLDFHQGWKGYFKMNVARQNNDSDSGAFVLQY CKHLALSQPFSFTQQDMPKLRRQIYKELCHCKLTV
>9ME8_2 Proline-, glutamic acid- and leucine-rich protein 1 (chains B) AFVHYDKEEASDVEISLE
PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex. Gordon, J., Kaminski, A.M., Bommu, S.R. et al. Sci Adv (2025) 11:eadw4603-eadw4603. DOI 10.1126/sciadv.adw4603 · PubMed
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