BRAFV600E Kinase Domain In Complex with Chemically Linked Vemurafenib Inhibitor VEM-3-VEM. Determined by X-ray diffraction at 2.19 Å resolution. Released 14 Sept 2016.
Explore 5JSM in 3D Show helices and sheets RCSB PDB PDBe
5JSM contains 63 α-helices and 40 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 451 | 1 | 1 |
| β-strand | 458-466 | 9 | 1 |
| β-strand | 469-475 | 7 | 1 |
| β-strand | 479-485 | 7 | 1 |
| α-helix | 492-507 | 16 | |
| β-strand | 513 | 1 | 2 |
| α-helix | 514-515 | 2 | |
| β-strand | 516-520 | 5 | 1 |
| β-strand | 526-530 | 5 | 1 |
| β-strand | 536 | 1 | 2 |
| α-helix | 537-539 | 3 | |
| α-helix | 540-544 | 5 | |
| α-helix | 550-569 | 20 | |
| α-helix | 579-581 | 3 | |
| β-strand | 582-584 | 3 | 2 |
| β-strand | 590-592 | 3 | 2 |
| α-helix | 615-619 | 5 | |
| α-helix | 622-626 | 5 | |
| α-helix | 635-651 | 17 | |
| α-helix | 662-671 | 10 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 705-706 | 2 | |
| α-helix | 707-719 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 447-450 | 4 | |
| β-strand | 451 | 1 | 3 |
| α-helix | 452-453 | 2 | |
| β-strand | 458-466 | 9 | 3 |
| β-strand | 469-475 | 7 | 3 |
| β-strand | 479-485 | 7 | 3 |
| α-helix | 492-507 | 16 | |
| β-strand | 513 | 1 | 4 |
| α-helix | 514-515 | 2 | |
| β-strand | 516-520 | 5 | 3 |
| β-strand | 526-530 | 5 | 3 |
| β-strand | 536 | 1 | 4 |
| α-helix | 537-538 | 2 | |
| α-helix | 539-543 | 5 | |
| α-helix | 550-569 | 20 | |
| α-helix | 579-581 | 3 | |
| β-strand | 582-584 | 3 | 4 |
| β-strand | 590-592 | 3 | 4 |
| α-helix | 598-601 | 4 | |
| α-helix | 617-619 | 3 | |
| α-helix | 622-625 | 4 | |
| α-helix | 635-651 | 17 | |
| α-helix | 662-671 | 10 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 705-706 | 2 | |
| α-helix | 707-719 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 451 | 1 | 5 |
| α-helix | 452-453 | 2 | |
| β-strand | 458-466 | 9 | 5 |
| β-strand | 469-475 | 7 | 5 |
| β-strand | 479-485 | 7 | 5 |
| α-helix | 492-507 | 16 | |
| β-strand | 513 | 1 | 6 |
| α-helix | 514-515 | 2 | |
| β-strand | 516-520 | 5 | 5 |
| β-strand | 526-530 | 5 | 5 |
| β-strand | 536 | 1 | 6 |
| α-helix | 537-542 | 6 | |
| α-helix | 550-569 | 20 | |
| α-helix | 579-581 | 3 | |
| β-strand | 582-584 | 3 | 6 |
| β-strand | 590-592 | 3 | 6 |
| α-helix | 622-625 | 4 | |
| α-helix | 635-651 | 17 | |
| α-helix | 664-670 | 7 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 705-706 | 2 | |
| α-helix | 707-719 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 447-450 | 4 | |
| β-strand | 451 | 1 | 7 |
| β-strand | 458-466 | 9 | 7 |
| β-strand | 469-475 | 7 | 7 |
| β-strand | 479-485 | 7 | 7 |
| α-helix | 492-507 | 16 | |
| β-strand | 513 | 1 | 8 |
| α-helix | 514-515 | 2 | |
| β-strand | 516-520 | 5 | 7 |
| β-strand | 526-530 | 5 | 7 |
| β-strand | 536 | 1 | 8 |
| α-helix | 537-539 | 3 | |
| α-helix | 540-544 | 5 | |
| α-helix | 550-569 | 20 | |
| α-helix | 579-581 | 3 | |
| β-strand | 582-584 | 3 | 8 |
| β-strand | 590-592 | 3 | 8 |
| α-helix | 617-619 | 3 | |
| α-helix | 622-625 | 4 | |
| α-helix | 635-651 | 17 | |
| α-helix | 664-671 | 8 | |
| α-helix | 678-680 | 3 | |
| α-helix | 687-696 | 10 | |
| α-helix | 701-703 | 3 | |
| α-helix | 705-706 | 2 | |
| α-helix | 707-719 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase B-raf | A, B, C, D | protein | 280 | Homo sapiens | P15056 (AlphaFold model) |
>5JSM_1 Serine/threonine-protein kinase B-raf (chains A, B, C, D) GSEFDDWEIPDGQITVGQRIGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQAFKNEVG VLRKTRHVNILLFMGYSTKPQLAIVTQWCEGSSLYHHLHASETKFEMKKLIDIARQTARG MDYLHAKSIIHRDLKSNNIFLHEDNTVKIGDFGLATEKSRWSGSHQFEQLSGSILWMAPE VIRMQDSNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIEMVGRGSLSPDLSKVRS NCPKRMKRLMAECLKKKRDERPSFPRILAEIEELARELSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| BEN | Benzamidine | C7 H8 N2 | 2 |
| EOH | Ethanol | C2 H6 O | 3 |
| 6NB | N,N'-{ethane-1,2-diylbis[oxyethane-2,1-diyloxy-4,1-phenylene-1H-pyrrolo[2,3-b]p… | C52 H48 F4 N6 O10 S2 | 2 |
Water and common crystallization additives (DMS, CL, GOL) are not listed.
Chemically Linked Vemurafenib Inhibitors Promote an Inactive BRAF(V600E) Conformation. Grasso, M., Estrada, M.A., Ventocilla, C. et al. ACS Chem Biol (2016) 11:2876-2888. DOI 10.1021/acschembio.6b00529 · PubMed
Other PDB entries of the same protein (UniProt P15056 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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