Structure of Epac2 in complex with cyclic-AMP and Rap. Determined by X-ray diffraction at 2.2 Å resolution. Released 29 Jul 2008.
Explore 3CF6 in 3D Show helices and sheets RCSB PDB PDBe
3CF6 contains 41 α-helices and 32 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 | 311-315 | 5 | |
| α-helix | 318-320 | 3 | |
| α-helix | 323-333 | 11 | |
| α-helix | 337-339 | 3 | |
| α-helix | 344-351 | 8 | |
| β-strand | 355-359 | 5 | 1 |
| β-strand | 365-367 | 3 | 2 |
| β-strand | 372 | 1 | 3 |
| β-strand | 375-381 | 7 | 1 |
| β-strand | 383-388 | 6 | 2 |
| β-strand | 392-398 | 7 | 2 |
| β-strand | 402-403 | 2 | 1 |
| α-helix | 405-410 | 6 | |
| β-strand | 413 | 1 | 3 |
| β-strand | 417-420 | 4 | 2 |
| β-strand | 425-431 | 7 | 1 |
| α-helix | 432-438 | 7 | |
| β-strand | 447-451 | 5 | 4 |
| β-strand | 454-461 | 8 | 4 |
| β-strand | 480-485 | 6 | 4 |
| α-helix | 487-496 | 10 | |
| α-helix | 502-504 | 3 | |
| α-helix | 505-522 | 18 | |
| α-helix | 525-536 | 12 | |
| α-helix | 545-570 | 26 | |
| α-helix | 571-576 | 6 | |
| α-helix | 578-598 | 21 | |
| α-helix | 604-611 | 8 | |
| β-strand | 651-657 | 7 | 5 |
| β-strand | 663-669 | 7 | 5 |
| β-strand | 673 | 1 | 6 |
| α-helix | 674-685 | 12 | |
| β-strand | 691-696 | 6 | 5 |
| β-strand | 702-704 | 3 | 5 |
| α-helix | 705-706 | 2 | |
| β-strand | 710 | 1 | 6 |
| α-helix | 713-715 | 3 | |
| β-strand | 721-726 | 6 | 5 |
| α-helix | 727-732 | 6 | |
| α-helix | 737-739 | 3 | |
| α-helix | 747-750 | 4 | |
| α-helix | 755-771 | 17 | |
| α-helix | 775-783 | 9 | |
| α-helix | 785-787 | 3 | |
| α-helix | 793-814 | 22 | |
| α-helix | 819-838 | 20 | |
| β-strand | 841 | 1 | 7 |
| α-helix | 842-852 | 11 | |
| α-helix | 855-858 | 4 | |
| α-helix | 861-865 | 5 | |
| α-helix | 869-880 | 12 | |
| α-helix | 885-897 | 13 | |
| β-strand | 903 | 1 | 7 |
| α-helix | 906-919 | 14 | |
| β-strand | 923-924 | 2 | 4 |
| β-strand | 927-929 | 3 | 4 |
| α-helix | 930-946 | 17 | |
| α-helix | 963-969 | 7 | |
| α-helix | 978-988 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 8 |
| α-helix | 16-24 | 9 | |
| β-strand | 41-43 | 3 | 8 |
| β-strand | 52-57 | 6 | 8 |
| α-helix | 65-74 | 10 | |
| β-strand | 77-83 | 7 | 8 |
| α-helix | 87-91 | 5 | |
| α-helix | 93-103 | 11 | |
| β-strand | 111-116 | 6 | 8 |
| α-helix | 128-133 | 6 | |
| β-strand | 143-145 | 3 | 8 |
| β-strand | 147 | 1 | 9 |
| β-strand | 152 | 1 | 9 |
| α-helix | 154-163 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rap guanine nucleotide exchange factor (GEF) 4 | E | protein | 694 | Mus musculus | A2ASW3 |
| Ras-related protein Rap-1b | R | protein | 167 | Homo sapiens | P61224 (AlphaFold model) |
>3CF6_1 Rap guanine nucleotide exchange factor (GEF) 4 (chains E) GSPESFPDAHMRMILRKPPGQRTVDDLEIIYDELLHIKALSHLSTTVKRELAGVLIFESH AKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDDFGKLALVNDAPRAASIV LREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKVPAGNRAANQGNSQPQQK YTVMSGTPEKILEHFLETIRLEPSLNEATDSVLNDFVMMHCVFMPNTQLCPALVAHYHAQ PSQGTEQERMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVAMAFLEEFYVSVSDDARMMA AFKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQKRQPIRGSDEVLFKVYCI DHTYTTIRVPVAASVKEVISAVADKLGSGEGLIIVKMNSGGEKVVLKSNDVSVFTTLTIN GRLFACPREQFDSLTPLPEQEGPTTGTVGTFELMSSKDLAYQMTTYDWELFNCVHELELI YHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEVCLCSQLSKRVQLLKKFIKIAAHCKEY KNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLMDPSRNHRAYRLTAAKLE PPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTARTVRYYRSQPFNPDAAQAN KNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP
>3CF6_2 Ras-related protein Rap-1b (chains R) MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAG TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDL EDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINR
| ID | Name | Formula | Copies |
|---|---|---|---|
| SP1 | 6-(6-amino-purin-9-yl)-2-thioxo-tetrahydro-2-FURO[3,2-D][1,3,2]DIOXAPHOSPHININE… | C10 H12 N5 O5 P S | 2 |
Water and common crystallization additives (SO4) are not listed.
Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B. Rehmann, H., Arias-Palomo, E., Hadders, M.A. et al. Nature (2008) 455:124-127. DOI 10.1038/nature07187 · PubMed
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