Fem-1 homolog B (FEM1B) in complex with VU0421763. Determined by X-ray diffraction at 2.93 Å resolution. Released 26 Nov 2025.
Explore 9PQ9 in 3D Show helices and sheets RCSB PDB PDBe
9PQ9 contains 40 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 | 29-36 | 8 | |
| β-strand | 40 | 1 | 1 |
| β-strand | 46 | 1 | 2 |
| β-strand | 47 | 1 | 1 |
| α-helix | 49-55 | 7 | |
| α-helix | 59-69 | 11 | |
| β-strand | 76-80 | 5 | 2 |
| β-strand | 85-90 | 6 | 2 |
| 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 | |
| β-strand | 183 | 1 | 3 |
| β-strand | 189 | 1 | 3 |
| α-helix | 190-196 | 7 | |
| α-helix | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-241 | 10 | |
| α-helix | 246-262 | 17 | |
| α-helix | 269-283 | 15 | |
| α-helix | 300-302 | 3 | |
| α-helix | 311-315 | 5 | |
| α-helix | 321-335 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-14 | 13 | |
| α-helix | 17-24 | 8 | |
| α-helix | 29-36 | 8 | |
| β-strand | 40 | 1 | 4 |
| β-strand | 46 | 1 | 5 |
| β-strand | 47 | 1 | 4 |
| α-helix | 49-55 | 7 | |
| α-helix | 59-69 | 11 | |
| β-strand | 76-81 | 6 | 5 |
| β-strand | 84-90 | 7 | 5 |
| 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 | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-239 | 8 | |
| α-helix | 246-262 | 17 | |
| α-helix | 269-283 | 15 | |
| α-helix | 300-302 | 3 | |
| α-helix | 311-315 | 5 | |
| 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) |
>9PQ9_1 Protein fem-1 homolog B (chains A, B) GHMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGH AKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTT VTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA DPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELL LSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPP IHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGGGGSGGGSKKRLLLGLDR
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1CI7 | 6-(propylsulfanyl)-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one | C8 H10 N4 O S | 2 |
Water and common crystallization additives (SO4) are not listed.
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:
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