Structure of Ephexin4 IDPSH. Determined by X-ray diffraction at 3.0 Å resolution. Released 24 Feb 2021.
Explore 7CSP in 3D Show helices and sheets RCSB PDB PDBe
7CSP contains 47 α-helices and 33 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 | 220-222 | 3 | |
| α-helix | 226-228 | 3 | |
| α-helix | 273-276 | 4 | |
| α-helix | 284-310 | 27 | |
| α-helix | 311-315 | 5 | |
| α-helix | 318-321 | 4 | |
| α-helix | 326-333 | 8 | |
| α-helix | 336-356 | 21 | |
| α-helix | 364-373 | 10 | |
| α-helix | 376-383 | 8 | |
| α-helix | 385-398 | 14 | |
| α-helix | 400-411 | 12 | |
| α-helix | 420-424 | 5 | |
| α-helix | 426-443 | 18 | |
| α-helix | 449-488 | 40 | |
| β-strand | 489-490 | 2 | 1 |
| β-strand | 506-514 | 9 | 1 |
| α-helix | 519-521 | 3 | |
| β-strand | 529-535 | 7 | 1 |
| β-strand | 538-546 | 9 | 1 |
| β-strand | 549-557 | 9 | 1 |
| α-helix | 558-560 | 3 | |
| β-strand | 561-565 | 5 | 1 |
| α-helix | 566-570 | 5 | |
| β-strand | 586-591 | 6 | 1 |
| β-strand | 600-605 | 6 | 1 |
| α-helix | 609-619 | 11 | |
| α-helix | 625-630 | 6 | |
| α-helix | 632-634 | 3 | |
| α-helix | 636 | 1 | |
| β-strand | 637-640 | 4 | 2 |
| β-strand | 644 | 1 | 3 |
| β-strand | 651 | 1 | 2 |
| β-strand | 654 | 1 | 3 |
| β-strand | 659-666 | 8 | 2 |
| β-strand | 669-674 | 6 | 2 |
| β-strand | 680-684 | 5 | 2 |
| α-helix | 685-687 | 3 | |
| β-strand | 688-691 | 4 | 2 |
| α-helix | 694-707 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 220-222 | 3 | |
| α-helix | 267-269 | 3 | |
| α-helix | 271-276 | 6 | |
| α-helix | 284-310 | 27 | |
| α-helix | 311-315 | 5 | |
| α-helix | 318-321 | 4 | |
| α-helix | 326-333 | 8 | |
| α-helix | 336-356 | 21 | |
| α-helix | 364-373 | 10 | |
| α-helix | 376-398 | 23 | |
| α-helix | 400-411 | 12 | |
| α-helix | 421-424 | 4 | |
| α-helix | 426-443 | 18 | |
| α-helix | 449-488 | 40 | |
| β-strand | 489-490 | 2 | 4 |
| α-helix | 491-493 | 3 | |
| β-strand | 506-514 | 9 | 4 |
| β-strand | 529-535 | 7 | 4 |
| β-strand | 538-544 | 7 | 4 |
| β-strand | 550-557 | 8 | 4 |
| α-helix | 558-560 | 3 | |
| β-strand | 561-565 | 5 | 4 |
| α-helix | 566-570 | 5 | |
| β-strand | 586-591 | 6 | 4 |
| β-strand | 594 | 1 | 4 |
| β-strand | 600-605 | 6 | 4 |
| α-helix | 609-619 | 11 | |
| α-helix | 621-627 | 7 | |
| α-helix | 628-634 | 7 | |
| α-helix | 636 | 1 | |
| β-strand | 637-640 | 4 | 5 |
| β-strand | 644 | 1 | 6 |
| β-strand | 651 | 1 | 5 |
| β-strand | 654 | 1 | 6 |
| β-strand | 659-666 | 8 | 5 |
| β-strand | 669-674 | 6 | 5 |
| β-strand | 680-684 | 5 | 5 |
| α-helix | 685-687 | 3 | |
| β-strand | 688-690 | 3 | 5 |
| α-helix | 694-707 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho guanine nucleotide exchange factor 16 | A, B | protein | 500 | Mus musculus | Q3U5C8 (AlphaFold model) |
>7CSP_1 Rho guanine nucleotide exchange factor 16 (chains A, B) GPGSEFHKGSFKDDPQLYQEIRERGLNTSHESDDDILDETTIVVKSYRPAQLTWSQLPEV LESGVLDTLSTEERKRQEAIFEILTSEFSYLHSLSILVTEFLQSRELRATMTQTEHHHLF SNILDVMSASQKFFEALEQRHKAQVCVEDISDILEDHAQHHFHPYIAYCSNEVYQQRTLQ KLSNSNAAFRDVLKEIEKRPACGGLPMISFLILPMQRVTRLPLLTDTLCLKTQGHPERYK AASQALKAISKLVKQCNEGAHKMERTEQIYTLNMQLDFGKVKSLPLISASRWLLKRGELF LLEESSIFRKIASRPTCYLFLFNDVLVVTKKKSEESYLVQDYAQLDHVQVRKLEPSEPLL PGGSSRSSSVPYPFQVNLLHNSEGRQEQILLSSDSASDRARWITALTYKERQWQGITNKG ELPQVEVTKAYFAKQADEITLQQADIVLVLQEEDGWLHGERLRDGETGWFPESFAHSITS RVAVEGNVRRMERLRVETDV
Double inhibition and activation mechanisms of Ephexin family RhoGEFs. Zhang, M., Lin, L., Wang, C. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2024465118 · PubMed
Other PDB entries of the same protein (UniProt Q3U5C8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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