4R3E: PDB entry 4R3E

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.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,588
Mol. weight
20.41 kDa
Released
19 Nov 2014

Explore 4R3E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix8-114
β-strand1211
β-strand14-1962
β-strand22-2872
β-strand2911
α-helix34-4512
β-strand52-5322
β-strand56-5832
β-strand62-6542
β-strand8313
β-strand98-10142
β-strand10913
β-strand113-11642
α-helix121-1233
β-strand129-13352
α-helix135-1373
α-helix138-1436
β-strand14914
α-helix151-1533
β-strand15514
β-strand160-16892

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Peptidyl-prolyl cis-trans isomerase CWC27 homologAprotein180Homo sapiensQ6UX04 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4R3E_1 Peptidyl-prolyl cis-trans isomerase CWC27 homolog (chains A)
GAMSNIYIQEPPTNGKVLLKTTAGDIDIELWSKEAPKACRNFIQLCLEAYYDNTIFHRVV
PGFIVQGGDPTGTGSGGESIYGAPFKDEFHSRLRFNRRGLVAMANAGSHDNGSQFFFTLG
RADELNNKHTIFGKVTGDTVYNMLRLSEVDIDDDERPHNPHKIKSCEVLFNPFDDIIPRE

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 4R3E 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.