WWP1 WW2-2,3-linker-WW3-WW4-HECT (WWP1-2L34H) with ordered WW2 domain. Determined by X-ray diffraction at 3.0 Å resolution. Released 15 May 2024.
Explore 9EQK in 3D Show helices and sheets RCSB PDB PDBe
9EQK contains 59 α-helices and 46 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 | 9-12 | 4 | |
| β-strand | 15-19 | 5 | 1 |
| β-strand | 25-29 | 5 | 1 |
| β-strand | 36 | 1 | 1 |
| α-helix | 42-57 | 16 | |
| α-helix | 61-67 | 7 | |
| α-helix | 75-77 | 3 | |
| α-helix | 85-87 | 3 | |
| β-strand | 90-94 | 5 | 2 |
| β-strand | 99-103 | 5 | 2 |
| β-strand | 108-110 | 3 | 2 |
| α-helix | 125-127 | 3 | |
| β-strand | 130-133 | 4 | 3 |
| β-strand | 141-144 | 4 | 3 |
| β-strand | 149 | 1 | 3 |
| α-helix | 175-187 | 13 | |
| β-strand | 194-199 | 6 | 4 |
| α-helix | 206-209 | 4 | |
| α-helix | 217-221 | 5 | |
| β-strand | 223-228 | 6 | 4 |
| α-helix | 236-250 | 15 | |
| α-helix | 254-256 | 3 | |
| β-strand | 259-263 | 5 | 5 |
| β-strand | 267-271 | 5 | 5 |
| α-helix | 273-277 | 5 | |
| α-helix | 281-297 | 17 | |
| α-helix | 308-314 | 7 | |
| α-helix | 321-327 | 7 | |
| α-helix | 329-339 | 11 | |
| β-strand | 351 | 1 | 6 |
| β-strand | 353-355 | 3 | 7 |
| β-strand | 364-366 | 3 | 7 |
| α-helix | 371-373 | 3 | |
| β-strand | 375 | 1 | 6 |
| α-helix | 381-394 | 14 | |
| α-helix | 398-409 | 12 | |
| α-helix | 414-417 | 4 | |
| α-helix | 422-429 | 8 | |
| α-helix | 433-435 | 3 | |
| α-helix | 437-442 | 6 | |
| β-strand | 445-447 | 3 | 8 |
| α-helix | 454-465 | 12 | |
| α-helix | 468-478 | 11 | |
| α-helix | 483-485 | 3 | |
| α-helix | 489-491 | 3 | |
| β-strand | 493-495 | 3 | 9 |
| β-strand | 497-498 | 2 | 9 |
| β-strand | 502-504 | 3 | 8 |
| β-strand | 514-516 | 3 | 8 |
| α-helix | 517-519 | 3 | |
| β-strand | 521-523 | 3 | 8 |
| α-helix | 530-542 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-12 | 3 | |
| β-strand | 15-19 | 5 | 10 |
| β-strand | 25-29 | 5 | 10 |
| β-strand | 35-36 | 2 | 10 |
| α-helix | 42-59 | 18 | |
| α-helix | 62-65 | 4 | |
| α-helix | 67-72 | 6 | |
| α-helix | 86-87 | 2 | |
| β-strand | 90-94 | 5 | 11 |
| β-strand | 100-104 | 5 | 11 |
| β-strand | 110-111 | 2 | 11 |
| β-strand | 130-134 | 5 | 12 |
| β-strand | 140-144 | 5 | 12 |
| β-strand | 149-151 | 3 | 12 |
| α-helix | 175-187 | 13 | |
| β-strand | 194-199 | 6 | 13 |
| α-helix | 204-209 | 6 | |
| α-helix | 217-221 | 5 | |
| β-strand | 223-228 | 6 | 13 |
| α-helix | 237-250 | 14 | |
| α-helix | 254-256 | 3 | |
| β-strand | 259-261 | 3 | 14 |
| β-strand | 269-271 | 3 | 14 |
| α-helix | 273-277 | 5 | |
| α-helix | 281-297 | 17 | |
| α-helix | 308-314 | 7 | |
| α-helix | 317-319 | 3 | |
| α-helix | 321-325 | 5 | |
| α-helix | 329-340 | 12 | |
| α-helix | 343-345 | 3 | |
| β-strand | 351 | 1 | 15 |
| β-strand | 353-357 | 5 | 16 |
| β-strand | 362-366 | 5 | 16 |
| α-helix | 371-373 | 3 | |
| β-strand | 375 | 1 | 15 |
| α-helix | 381-392 | 12 | |
| α-helix | 398-411 | 14 | |
| α-helix | 414-417 | 4 | |
| α-helix | 422-430 | 9 | |
| α-helix | 433-435 | 3 | |
| α-helix | 437-442 | 6 | |
| β-strand | 444-447 | 4 | 17 |
| α-helix | 454-464 | 11 | |
| α-helix | 468-479 | 12 | |
| α-helix | 489-491 | 3 | |
| β-strand | 493 | 1 | 18 |
| β-strand | 498 | 1 | 18 |
| β-strand | 501-505 | 5 | 17 |
| α-helix | 512-513 | 2 | |
| β-strand | 514-516 | 3 | 17 |
| α-helix | 517-519 | 3 | |
| β-strand | 521-524 | 4 | 17 |
| α-helix | 530-540 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| NEDD4-like E3 ubiquitin-protein ligase WWP1 | A, B | protein | 550 | Homo sapiens | Q9H0M0 (AlphaFold model) |
>9EQK_1 NEDD4-like E3 ubiquitin-protein ligase WWP1 (chains A, B) GPGSEFRPQPLPPGWERRVDDRRRVYYVDHNTRTTTWQRPTMESVRNFEQWQSQRNQLQG AMQQFNQRYLYSASMLAAENDPYGPLPPGWEKRVDSTDRVYFVNHNTKTTQWEDPRTQGL QNEEPLPEGWEIRYTREGVRYFVDHNTRTTTFKDPRNGKSSVTKGGPQIAYERGFRWKLA HFRYLCQSNALPSHVKINVSRQTLFEDSFQQIMALKPYDLRRRLYVIFRGEEGLDYGGLA REWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASTINPDHLSYFCFIGRFIAMALFHGK FIDTGFSLPFYKRMLSKKLTIKDLESIDTEFYNSLIWIRDNNIEECGLEMYFSVDMEILG KVTSHDLKLGGSNILVTEENKDEYIGLMTEWRFSRGVQEQTKAFLDGFNEVVPLQWLQYF DEKELEVMLCGMQEVDLADWQRNTVYRHYTRNSKQIIWFWQFVKETDNEVRMRLLQFVTG TCRLPLGGFAELMGSNGPQKFCIEKVGKDTWLPRSHTCFNRLDLPPYKSYEQLKEKLLFA IEETEGFGQE
Expanding the inhibitor space of the WWP1 and WWP2 HECT E3 ligases. Dudey, A.P., Rigby, J.M., Hughes, G.R. et al. J Enzyme Inhib Med Chem (2024) 39:2394895-2394895. DOI 10.1080/14756366.2024.2394895 · PubMed
Other PDB entries of the same protein (UniProt Q9H0M0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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