Fem-1 homolog B (FEM1B) in complex with VU0081201. Determined by X-ray diffraction at 3.0 Å resolution. Released 26 Nov 2025.
Explore 9PWJ in 3D Show helices and sheets RCSB PDB PDBe
9PWJ contains 44 α-helices and 11 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 | 4-14 | 11 | |
| 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 | 49-56 | 8 | |
| α-helix | 59-63 | 5 | |
| α-helix | 64-68 | 5 | |
| β-strand | 78-81 | 4 | 2 |
| β-strand | 84-87 | 4 | 2 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| 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 | 232-239 | 8 | |
| α-helix | 247-262 | 16 | |
| α-helix | 269-283 | 15 | |
| α-helix | 295-298 | 4 | |
| α-helix | 300-302 | 3 | |
| α-helix | 311-317 | 7 | |
| 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 | 40-42 | 3 | 3 |
| β-strand | 45-47 | 3 | 3 |
| α-helix | 49-56 | 8 | |
| α-helix | 59-63 | 5 | |
| α-helix | 64-68 | 5 | |
| β-strand | 77-81 | 5 | 4 |
| β-strand | 84-89 | 6 | 4 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| α-helix | 157-164 | 8 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-196 | 7 | |
| α-helix | 200-207 | 8 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-239 | 8 | |
| α-helix | 247-259 | 13 | |
| α-helix | 270-283 | 14 | |
| α-helix | 295-298 | 4 | |
| β-strand | 299 | 1 | 5 |
| β-strand | 305 | 1 | 5 |
| α-helix | 311-316 | 6 | |
| α-helix | 317-319 | 3 | |
| α-helix | 321-336 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein fem-1 homolog B | A, B | protein | 357 | Homo sapiens | Q9UK73 (AlphaFold model) |
>9PWJ_1 Protein fem-1 homolog B (chains A, B) GHMEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGH AKVVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTT VTNSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRA DPNAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELL LSHADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPP IHAYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGGGGSGGGSKKRLLLGLDR
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1CL1 | 3-(2-oxopyrrolidin-1-yl)benzoic acid | C11 H11 N O3 | 1 |
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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