Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Nov 2014.
Explore 4R3E in 3D Show helices and sheets RCSB PDB PDBe
4R3E contains 6 α-helices and 15 β-strands across 1 chain. 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 | 8-11 | 4 | |
| β-strand | 12 | 1 | 1 |
| β-strand | 14-19 | 6 | 2 |
| β-strand | 22-28 | 7 | 2 |
| β-strand | 29 | 1 | 1 |
| α-helix | 34-45 | 12 | |
| β-strand | 52-53 | 2 | 2 |
| β-strand | 56-58 | 3 | 2 |
| β-strand | 62-65 | 4 | 2 |
| β-strand | 83 | 1 | 3 |
| β-strand | 98-101 | 4 | 2 |
| β-strand | 109 | 1 | 3 |
| β-strand | 113-116 | 4 | 2 |
| α-helix | 121-123 | 3 | |
| β-strand | 129-133 | 5 | 2 |
| α-helix | 135-137 | 3 | |
| α-helix | 138-143 | 6 | |
| β-strand | 149 | 1 | 4 |
| α-helix | 151-153 | 3 | |
| β-strand | 155 | 1 | 4 |
| β-strand | 160-168 | 9 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase CWC27 homolog | A | protein | 180 | Homo sapiens | Q6UX04 (AlphaFold model) |
>4R3E_1 Peptidyl-prolyl cis-trans isomerase CWC27 homolog (chains A) GAMSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVV PGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNRRGLVAMANAGSHDNGSQFFFTLG RADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVLFNPFDDIIPRE
Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27. Ulrich, A., Wahl, M.C. Acta Crystallogr D Biol Crystallogr (2014) 70:3110-3123. DOI 10.1107/S1399004714021695 · PubMed
Other PDB entries of the same protein (UniProt Q6UX04 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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