Structure of SMCR8 bound FEM1B. Determined by X-ray diffraction at 2.8 Å resolution. Released 12 May 2021.
Explore 7EL6 in 3D Show helices and sheets RCSB PDB PDBe
7EL6 contains 46 α-helices and 10 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 | 40-41 | 2 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 49-56 | 8 | |
| α-helix | 59-63 | 5 | |
| α-helix | 64-68 | 5 | |
| α-helix | 69 | 1 | |
| β-strand | 76-81 | 6 | 2 |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| α-helix | 157-163 | 7 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-197 | 8 | |
| α-helix | 200-208 | 9 | |
| α-helix | 211-213 | 3 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-241 | 10 | |
| α-helix | 246-259 | 14 | |
| α-helix | 269-283 | 15 | |
| α-helix | 292-297 | 6 | |
| α-helix | 298-300 | 3 | |
| α-helix | 311-315 | 5 | |
| α-helix | 321-336 | 16 | |
| α-helix | 348-354 | 7 |
| 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 | 59-63 | 5 | |
| α-helix | 64-68 | 5 | |
| β-strand | 77-81 | 5 | 3 |
| β-strand | 84-89 | 6 | 3 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| α-helix | 157-163 | 7 | |
| α-helix | 167-175 | 9 | |
| α-helix | 190-197 | 8 | |
| α-helix | 200-208 | 9 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-241 | 10 | |
| α-helix | 247-259 | 13 | |
| α-helix | 269-283 | 15 | |
| β-strand | 302 | 1 | 4 |
| β-strand | 305 | 1 | 4 |
| α-helix | 311-315 | 5 | |
| α-helix | 321-335 | 15 | |
| α-helix | 348-354 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein fem-1 homolog B,Guanine nucleotide exchange protein SMCR8 | A, B | protein | 357 | Homo sapiens | Q8TEV9 (AlphaFold model), Q9UK73 (AlphaFold model) |
>7EL6_1 Protein fem-1 homolog B,Guanine nucleotide exchange protein SMCR8 (chains A, B) MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAK VVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVT NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP NAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLS HADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIH AYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGGGGSGGGSGSQKWKLIGLQR
Structural insights into SMCR8 C-degron recognition by FEM1B. Zhao, S., Ru, W., Chen, X. et al. Biochem Biophys Res Commun (2021) 557:236-239. DOI 10.1016/j.bbrc.2021.04.046 · PubMed
Other PDB entries of the same protein (UniProt Q8TEV9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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