Crystal structure of human G3BP1 in complex with Semliki Forest Virus nsP3-25 comprising two FGDF motives. Determined by X-ray diffraction at 1.92 Å resolution. Released 20 Jul 2016.
Explore 5FW5 in 3D Show helices and sheets RCSB PDB PDBe
5FW5 contains 15 α-helices and 15 β-strands across 3 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 | 5-7 | 3 | |
| α-helix | 8-25 | 18 | |
| α-helix | 27-33 | 7 | |
| β-strand | 34-42 | 9 | 1 |
| β-strand | 45 | 1 | 2 |
| β-strand | 51 | 1 | 2 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 1 |
| α-helix | 57-67 | 11 | |
| β-strand | 74-84 | 11 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-99 | 10 | 1 |
| β-strand | 106-116 | 11 | 1 |
| β-strand | 123-133 | 11 | 1 |
| α-helix | 134-136 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-25 | 18 | |
| α-helix | 27-33 | 7 | |
| β-strand | 34-42 | 9 | 3 |
| α-helix | 50-52 | 3 | |
| β-strand | 55-56 | 2 | 3 |
| α-helix | 58-67 | 10 | |
| β-strand | 74-84 | 11 | 3 |
| α-helix | 86-88 | 3 | |
| β-strand | 90-99 | 10 | 3 |
| α-helix | 103-105 | 3 | |
| β-strand | 106-116 | 11 | 3 |
| β-strand | 124-133 | 10 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 450-451 | 2 | 1 |
| α-helix | 454-455 | 2 | |
| α-helix | 458-463 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras gtpase-activating protein-binding protein 1 | A, B | protein | 140 | HOMO SAPIENS | Q13283 (AlphaFold model) |
| Non-structural protein 3 | C | protein | 25 | SEMLIKI FOREST VIRUS | P08411 (AlphaFold model) |
>5FW5_1 RAS GTPASE-ACTIVATING PROTEIN-BINDING PROTEIN 1 (chains A, B) SMVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQK EIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGS VANKFYVHNDIFRYQDEVFG
>5FW5_2 NON-STRUCTURAL PROTEIN 3 (chains C) LTFGDFDEHEVDALASGITFGDFDD
Combined structural, biochemical and cellular evidence demonstrates that both FGDF motifs in alphavirus nsP3 are required for efficient replication. Schulte, T., Liu, L., Panas, M.D. et al. Open Biol (2016) 6. DOI 10.1098/rsob.160078 · PubMed
Other PDB entries of the same protein (UniProt Q13283 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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