Crystal structure of Human ARS2 residues 147-270 + 408-763 with deletion of loop B. Determined by X-ray diffraction at 3.37 Å resolution. Released 9 May 2018.
Explore 6F7S in 3D Show helices and sheets RCSB PDB PDBe
6F7S contains 51 α-helices and 36 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 |
|---|---|---|---|
| α-helix | 152-156 | 5 | |
| α-helix | 166-190 | 25 | |
| α-helix | 195-201 | 7 | |
| α-helix | 203-230 | 28 | |
| β-strand | 239 | 1 | 1 |
| α-helix | 240-242 | 3 | |
| α-helix | 243-257 | 15 | |
| α-helix | 264-268 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 412-414 | 3 | |
| β-strand | 421-427 | 7 | 2 |
| α-helix | 433-441 | 9 | |
| β-strand | 446-451 | 6 | 2 |
| α-helix | 452-454 | 3 | |
| β-strand | 455 | 1 | 3 |
| α-helix | 456-458 | 3 | |
| β-strand | 461 | 1 | 3 |
| β-strand | 462-468 | 7 | 2 |
| α-helix | 474-481 | 8 | |
| β-strand | 485 | 1 | 4 |
| β-strand | 490 | 1 | 4 |
| β-strand | 493-496 | 4 | 2 |
| α-helix | 497-499 | 3 | |
| β-strand | 503-506 | 4 | 1 |
| α-helix | 508-511 | 4 | |
| α-helix | 513-534 | 22 | |
| α-helix | 551-554 | 4 | |
| α-helix | 561-565 | 5 | |
| α-helix | 602-617 | 16 | |
| β-strand | 621-622 | 2 | 5 |
| β-strand | 627-628 | 2 | 5 |
| β-strand | 642-645 | 4 | 1 |
| α-helix | 647-649 | 3 | |
| α-helix | 655-669 | 15 | |
| α-helix | 670-673 | 4 | |
| β-strand | 678 | 1 | 6 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-687 | 7 | |
| α-helix | 689-691 | 3 | |
| α-helix | 692-702 | 11 | |
| β-strand | 705-708 | 4 | 7 |
| β-strand | 711-713 | 3 | 7 |
| β-strand | 720-721 | 2 | 7 |
| α-helix | 724-734 | 11 | |
| α-helix | 736-754 | 19 | |
| β-strand | 755 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 421-427 | 7 | 9 |
| α-helix | 433-441 | 9 | |
| β-strand | 446-451 | 6 | 9 |
| α-helix | 452-454 | 3 | |
| β-strand | 455 | 1 | 10 |
| α-helix | 456-458 | 3 | |
| β-strand | 461 | 1 | 10 |
| β-strand | 462-468 | 7 | 9 |
| α-helix | 474-481 | 8 | |
| β-strand | 485 | 1 | 11 |
| β-strand | 490 | 1 | 11 |
| β-strand | 493-496 | 4 | 9 |
| α-helix | 497-499 | 3 | |
| β-strand | 503-506 | 4 | 8 |
| α-helix | 508-511 | 4 | |
| α-helix | 513-534 | 22 | |
| α-helix | 601-617 | 17 | |
| β-strand | 621-622 | 2 | 12 |
| β-strand | 627-628 | 2 | 12 |
| β-strand | 642-645 | 4 | 8 |
| α-helix | 647-649 | 3 | |
| α-helix | 655-669 | 15 | |
| α-helix | 670-673 | 4 | |
| β-strand | 678 | 1 | 13 |
| α-helix | 679-680 | 2 | |
| α-helix | 681-687 | 7 | |
| α-helix | 689-691 | 3 | |
| α-helix | 692-702 | 11 | |
| β-strand | 705-708 | 4 | 14 |
| β-strand | 711-713 | 3 | 14 |
| β-strand | 720-721 | 2 | 14 |
| α-helix | 724-734 | 11 | |
| α-helix | 736-754 | 19 | |
| β-strand | 755 | 1 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serrate RNA effector molecule homolog | A, B | protein | 124 | Homo sapiens | Q9BXP5 (AlphaFold model) |
| Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog | C, D | protein | 331 | Homo sapiens | Q9BXP5 (AlphaFold model) |
>6F7S_1 Serrate RNA effector molecule homolog (chains A, B) PVMKTFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEV GKRRQEARGALQNRLRVFLSLMETGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLR ILEQ
>6F7S_2 Serrate RNA effector molecule homolog,Serrate RNA effector molecule homolog (chains C, D) GLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVT FDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLI HTLDDRTQLWASEPGTPPLPTSLPSQNPILKNITDYLIEEGSGSGSERDEKLIKVLDKLL LYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGPMPPNRISHGEVLEWQKTFEEKLTPL LSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQELGKDKWLCPLSGKKFKGPEFVRKHIF NKHAEKIEEVKKEVAFFNNFLTDAKRPALPE
Structural analysis of human ARS2 as a platform for co-transcriptional RNA sorting. Schulze, W.M., Stein, F., Rettel, M. et al. Nat Commun (2018) 9:1701-1701. DOI 10.1038/s41467-018-04142-7 · PubMed
Other PDB entries of the same protein (UniProt Q9BXP5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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