Fem-1 homolog B (FEM1B) in complex with VU0417412. Determined by X-ray diffraction at 2.8 Å resolution. Released 26 Nov 2025.
Explore 9PW8 in 3D Show helices and sheets RCSB PDB PDBe
9PW8 contains 41 α-helices and 12 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 | 2-14 | 13 | |
| α-helix | 17-24 | 8 | |
| α-helix | 29-37 | 9 | |
| β-strand | 40-41 | 2 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 49-55 | 7 | |
| α-helix | 59-67 | 9 | |
| β-strand | 76-80 | 5 | 1 |
| β-strand | 85-90 | 6 | 1 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-141 | 8 | |
| α-helix | 157-163 | 7 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-196 | 7 | |
| α-helix | 200-207 | 8 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-238 | 7 | |
| α-helix | 248-262 | 15 | |
| α-helix | 269-279 | 11 | |
| α-helix | 294-297 | 4 | |
| β-strand | 301 | 1 | 2 |
| β-strand | 303 | 1 | 2 |
| α-helix | 311-316 | 6 | |
| α-helix | 321-335 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-13 | 12 | |
| α-helix | 17-24 | 8 | |
| α-helix | 29-35 | 7 | |
| β-strand | 40-42 | 3 | 3 |
| β-strand | 45-47 | 3 | 3 |
| α-helix | 49-55 | 7 | |
| α-helix | 59-67 | 9 | |
| β-strand | 76-81 | 6 | 3 |
| β-strand | 84-90 | 7 | 3 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-141 | 8 | |
| α-helix | 157-164 | 8 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-196 | 7 | |
| α-helix | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-238 | 7 | |
| α-helix | 247-262 | 16 | |
| α-helix | 269-281 | 13 | |
| α-helix | 294-297 | 4 | |
| β-strand | 301 | 1 | 4 |
| β-strand | 303 | 1 | 4 |
| α-helix | 311-316 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 321-335 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein fem-1 homolog B | A, B | protein | 357 | Homo sapiens | Q9UK73 (AlphaFold model) |
>9PW8_1 Protein fem-1 homolog B (chains A, B) GHMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGH AKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTT VTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA DPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELL LSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPP IHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGGGGSGGGSKKRLLLGLDR
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1CLY | N-(4-fluorophenyl)thiophene-2-carboxamide | C11 H8 F N O S | 2 |
Nuclear Magnetic Resonance-based fragment screen of the E3 ligase Fem-1 homolog B. Katinas, J.M., Amporndanai, K., Taylor, A.J. et al. Protein Sci (2025) 34:e70365-e70365. DOI 10.1002/pro.70365 · PubMed
Other PDB entries of the same protein (UniProt Q9UK73 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9PW8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.