Cyclophilin a complexed with a fragment of crk-ii. Determined by solution NMR. Released 9 Sept 2015.
Explore 2MS4 in 3D Show helices and sheets RCSB PDB PDBe
2MS4 contains 5 α-helices and 17 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 | 4 | 1 | |
| β-strand | 5-12 | 8 | 1 |
| β-strand | 15-24 | 10 | 1 |
| α-helix | 30-41 | 12 | |
| β-strand | 52-57 | 6 | 1 |
| β-strand | 61-65 | 5 | 1 |
| β-strand | 76 | 1 | 2 |
| β-strand | 77 | 1 | 3 |
| β-strand | 80 | 1 | 3 |
| β-strand | 83 | 1 | 4 |
| β-strand | 97-99 | 3 | 1 |
| β-strand | 102 | 1 | 4 |
| β-strand | 108 | 1 | 4 |
| β-strand | 110 | 1 | 2 |
| β-strand | 112-115 | 4 | 1 |
| α-helix | 120-122 | 3 | |
| α-helix | 127-128 | 2 | |
| β-strand | 130-134 | 5 | 1 |
| α-helix | 136-143 | 8 | |
| β-strand | 146 | 1 | 5 |
| β-strand | 152 | 1 | 5 |
| β-strand | 156-161 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase A | A | protein | 165 | Homo sapiens | P62937 (AlphaFold model) |
| Peptide | B | protein | 9 | P46108 (AlphaFold model) |
>2MS4_1 Peptidyl-prolyl cis-trans isomerase A (chains A) MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGF MCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTE WLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIADCGQLE
>2MS4_2 Peptide (chains B) PEPGPYAQP
Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway. Saleh, T., Jankowski, W., Sriram, G. et al. Nat Chem Biol (2016) 12:117-123. DOI 10.1038/nchembio.1981 · PubMed
Other PDB entries of the same protein (UniProt P62937 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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