Crystal structure analysis of catalytic subunit of human calcineurin. Determined by X-ray diffraction at 3.35 Å resolution. Released 3 Feb 2016.
Explore 5C1V in 3D Show helices and sheets RCSB PDB PDBe
5C1V contains 35 α-helices and 39 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 | 28-29 | 2 | 1 |
| α-helix | 31-34 | 4 | |
| β-strand | 35 | 1 | 2 |
| β-strand | 41 | 1 | 2 |
| α-helix | 43-50 | 8 | |
| β-strand | 55-56 | 2 | 1 |
| α-helix | 58-73 | 16 | |
| β-strand | 78-81 | 4 | 3 |
| α-helix | 82 | 1 | |
| α-helix | 84 | 1 | |
| β-strand | 85-88 | 4 | 4 |
| α-helix | 95-105 | 11 | |
| β-strand | 113-115 | 3 | 4 |
| α-helix | 126-139 | 14 | |
| β-strand | 144-146 | 3 | 4 |
| α-helix | 154-159 | 6 | |
| α-helix | 162-169 | 8 | |
| α-helix | 172-183 | 12 | |
| β-strand | 188-191 | 4 | 3 |
| β-strand | 195-198 | 4 | 3 |
| α-helix | 209-213 | 5 | |
| α-helix | 220-222 | 3 | |
| α-helix | 226-232 | 7 | |
| β-strand | 234-235 | 2 | 5 |
| β-strand | 248-250 | 3 | 5 |
| β-strand | 258-260 | 3 | 5 |
| α-helix | 262-271 | 10 | |
| β-strand | 276-279 | 4 | 3 |
| α-helix | 283-284 | 2 | |
| β-strand | 288-290 | 3 | 3 |
| α-helix | 292 | 1 | |
| β-strand | 293 | 1 | 6 |
| α-helix | 294 | 1 | |
| β-strand | 300 | 1 | 6 |
| β-strand | 302-305 | 4 | 3 |
| α-helix | 311-313 | 3 | |
| β-strand | 319-325 | 7 | 4 |
| β-strand | 328-334 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28-29 | 2 | 7 |
| α-helix | 31-34 | 4 | |
| β-strand | 35 | 1 | 8 |
| β-strand | 41 | 1 | 8 |
| α-helix | 43-50 | 8 | |
| β-strand | 55-56 | 2 | 7 |
| α-helix | 58-74 | 17 | |
| β-strand | 78-81 | 4 | 9 |
| α-helix | 82 | 1 | |
| α-helix | 84 | 1 | |
| β-strand | 85-88 | 4 | 4 |
| α-helix | 95-105 | 11 | |
| β-strand | 113-115 | 3 | 4 |
| α-helix | 126-139 | 14 | |
| β-strand | 144-146 | 3 | 4 |
| α-helix | 147-149 | 3 | |
| α-helix | 154-159 | 6 | |
| α-helix | 162-169 | 8 | |
| α-helix | 172-183 | 12 | |
| β-strand | 188-191 | 4 | 9 |
| β-strand | 195-198 | 4 | 9 |
| α-helix | 209-214 | 6 | |
| α-helix | 220-222 | 3 | |
| α-helix | 226-232 | 7 | |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 248-250 | 3 | 10 |
| β-strand | 258-260 | 3 | 10 |
| α-helix | 262-271 | 10 | |
| β-strand | 276-279 | 4 | 9 |
| α-helix | 291-292 | 2 | |
| β-strand | 293 | 1 | 11 |
| α-helix | 294 | 1 | |
| β-strand | 300 | 1 | 11 |
| β-strand | 302-304 | 3 | 9 |
| β-strand | 312-314 | 3 | 4 |
| β-strand | 321-322 | 2 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform | A, B | protein | 346 | Homo sapiens | Q08209 (AlphaFold model) |
>5C1V_1 Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (chains A, B) SEPKAIDPKLSTTDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKEGRLEESVA LRIITEGASILRQEKNLLDIDAPVTVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVD RGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMDA FDCLPLAALMNQQFLCVHGGLSPEINTLDDIRKLDRFKEPPAYGPMCDILWSDPLEDFGN EKTQEHFTHNTVRGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRKSQTTGFPS LITIFSAPNYLDVYNNKAAVLKYENNVMNIRQFNCSPHPSWAPNFD
Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization. Guasch, A., Aranguren-Ibanez, A., Perez-Luque, R. et al. PLoS One (2015) 10:e0134569-e0134569. DOI 10.1371/journal.pone.0134569 · PubMed
Other PDB entries of the same protein (UniProt Q08209 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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