MIRAS structure determination from hemihedrally twinned crystals. Determined by X-ray diffraction at 2.2 Å resolution. Released 11 Jan 2006.
Explore 2CA6 in 3D Show helices and sheets RCSB PDB PDBe
2CA6 contains 37 α-helices and 31 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 |
|---|---|---|---|
| β-strand | 3-5 | 3 | 1 |
| β-strand | 12-13 | 2 | 2 |
| α-helix | 19-22 | 4 | |
| α-helix | 26-30 | 5 | |
| β-strand | 36-38 | 3 | 1 |
| β-strand | 43-44 | 2 | 2 |
| α-helix | 46-54 | 9 | |
| β-strand | 64-66 | 3 | 1 |
| α-helix | 76-78 | 3 | |
| α-helix | 80-90 | 11 | |
| β-strand | 98-100 | 3 | 1 |
| α-helix | 111-120 | 10 | |
| β-strand | 126-128 | 3 | 1 |
| α-helix | 135-156 | 22 | |
| α-helix | 158-161 | 4 | |
| β-strand | 163-165 | 3 | 1 |
| α-helix | 173-175 | 3 | |
| α-helix | 176-185 | 10 | |
| β-strand | 191-193 | 3 | 1 |
| α-helix | 201-209 | 9 | |
| α-helix | 212-214 | 3 | |
| β-strand | 220-222 | 3 | 1 |
| α-helix | 229-239 | 11 | |
| α-helix | 240-242 | 3 | |
| β-strand | 248-250 | 3 | 1 |
| α-helix | 258-269 | 12 | |
| β-strand | 278-280 | 3 | 1 |
| β-strand | 287 | 1 | 3 |
| α-helix | 288-301 | 14 | |
| β-strand | 307-309 | 3 | 1 |
| β-strand | 314 | 1 | 3 |
| α-helix | 320-332 | 13 | |
| β-strand | 336-337 | 2 | 1 |
| α-helix | 338-339 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 4 |
| β-strand | 12-13 | 2 | 5 |
| α-helix | 20-22 | 3 | |
| β-strand | 36-38 | 3 | 4 |
| β-strand | 43-44 | 2 | 5 |
| α-helix | 46-58 | 13 | |
| β-strand | 64-66 | 3 | 4 |
| β-strand | 71 | 1 | 5 |
| α-helix | 76-78 | 3 | |
| α-helix | 80-90 | 11 | |
| β-strand | 98-100 | 3 | 4 |
| α-helix | 108-110 | 3 | |
| α-helix | 111-118 | 8 | |
| β-strand | 126-128 | 3 | 4 |
| α-helix | 135-156 | 22 | |
| α-helix | 158-161 | 4 | |
| β-strand | 163-165 | 3 | 4 |
| α-helix | 173-175 | 3 | |
| α-helix | 176-185 | 10 | |
| β-strand | 191-193 | 3 | 4 |
| α-helix | 201-206 | 6 | |
| α-helix | 207-211 | 5 | |
| α-helix | 212-214 | 3 | |
| β-strand | 220-222 | 3 | 4 |
| α-helix | 229-239 | 11 | |
| α-helix | 240-242 | 3 | |
| β-strand | 248-250 | 3 | 4 |
| α-helix | 258-268 | 11 | |
| β-strand | 278-280 | 3 | 4 |
| α-helix | 288-301 | 14 | |
| β-strand | 307-309 | 3 | 4 |
| α-helix | 321-332 | 12 | |
| β-strand | 336-337 | 2 | 4 |
| α-helix | 338-339 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ran gtpase-activating protein 1 | A, B | protein | 386 | SCHIZOSACCHAROMYCES POMBE | P41391 (AlphaFold model) |
>2CA6_1 RAN GTPASE-ACTIVATING PROTEIN 1 (chains A, B) MARFSIEGKSLKLDAITTEDEKSVFAVLLEDDSVKEIVLSGNTIGTEAARWLSENIASKK DLEIAEFSDIFTGRVKDEIPEALRLLLQALLKCPKLHTVRLSDNAFGPTAQEPLIDFLSK HTPLEHLYLHNNGLGPQAGAKIARALQELAVNKKAKNAPPLRSIICGRNRLENGSMKEWA KTFQSHRLLHTVKMVQNGIRPEGIEHLLLEGLAYCQELKVLDLQDNTFTHLGSSALAIAL KSWPNLRELGLNDCLLSARGAAAVVDAFSKLENIGLQTLRLQYNEIELDAVRTLKTVIDE KMPDLLFLELNGNRFSEEDDVVDEIREVFSTRGRGELDELDDMEELTDEEEEDEEEEAES QSPEPETSEEEKEDKELADELSKAHI
Detecting and Overcoming Hemihedral Twinning During the Mir Structure Determination of RNA1P. Hillig, R.C., Renault, L. Acta Crystallogr D Biol Crystallogr (2006) 62:750. DOI 10.1107/S0907444906016222 · PubMed
Other PDB entries of the same protein (UniProt P41391 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2CA6 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.