Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with cantharidic acid. Determined by X-ray diffraction at 1.4 Å resolution. Released 29 Sept 2009.
Explore 3H62 in 3D Show helices and sheets RCSB PDB PDBe
3H62 contains 26 α-helices and 36 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 | 182 | 1 | 6 |
| β-strand | 185 | 1 | 6 |
| α-helix | 188-199 | 12 | |
| α-helix | 206-221 | 16 | |
| β-strand | 226-229 | 4 | 7 |
| β-strand | 236-240 | 5 | 8 |
| α-helix | 247-257 | 11 | |
| β-strand | 261 | 1 | 9 |
| β-strand | 264 | 1 | 9 |
| β-strand | 266-269 | 4 | 8 |
| α-helix | 279-292 | 14 | |
| β-strand | 297-300 | 4 | 8 |
| α-helix | 307-313 | 7 | |
| α-helix | 315-322 | 8 | |
| α-helix | 325-335 | 11 | |
| β-strand | 341-344 | 4 | 7 |
| β-strand | 348-351 | 4 | 7 |
| α-helix | 363-367 | 5 | |
| α-helix | 374-376 | 3 | |
| α-helix | 380-386 | 7 | |
| β-strand | 388-389 | 2 | 10 |
| β-strand | 395-397 | 3 | 10 |
| β-strand | 404-406 | 3 | 10 |
| α-helix | 408-417 | 10 | |
| β-strand | 422-425 | 4 | 7 |
| β-strand | 434-437 | 4 | 7 |
| α-helix | 438-440 | 3 | |
| β-strand | 442-445 | 4 | 7 |
| α-helix | 451-453 | 3 | |
| β-strand | 459-465 | 7 | 8 |
| β-strand | 468-476 | 9 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 182 | 1 | 1 |
| β-strand | 185 | 1 | 1 |
| α-helix | 188-199 | 12 | |
| α-helix | 206-221 | 16 | |
| β-strand | 226-229 | 4 | 2 |
| β-strand | 236-240 | 5 | 3 |
| α-helix | 247-257 | 11 | |
| β-strand | 261 | 1 | 4 |
| β-strand | 264 | 1 | 4 |
| β-strand | 266-269 | 4 | 3 |
| α-helix | 279-292 | 14 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 307-313 | 7 | |
| α-helix | 315-322 | 8 | |
| α-helix | 325-335 | 11 | |
| β-strand | 341-344 | 4 | 2 |
| β-strand | 348-350 | 3 | 2 |
| α-helix | 363-368 | 6 | |
| α-helix | 375-376 | 2 | |
| α-helix | 380-386 | 7 | |
| β-strand | 388-389 | 2 | 5 |
| β-strand | 395-397 | 3 | 5 |
| β-strand | 404-406 | 3 | 5 |
| α-helix | 408-418 | 11 | |
| β-strand | 422-425 | 4 | 2 |
| β-strand | 434-437 | 4 | 2 |
| α-helix | 438-440 | 3 | |
| β-strand | 442-445 | 4 | 2 |
| α-helix | 451-453 | 3 | |
| β-strand | 459-465 | 7 | 3 |
| β-strand | 468-476 | 9 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein phosphatase 5 | B, C | protein | 315 | Homo sapiens | P53041 (AlphaFold model) |
>3H62_1 Serine/threonine-protein phosphatase 5 (chains B, C) YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETE KITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPD HFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGL FSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQ FTAVPHPNVKPMAYA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 4 |
| NHC | (1R,2S,3R,4S)-2,3-dimethyl-7-oxabicyclo[2.2.1]heptane-2,3-dicarboxylic acid | C10 H14 O5 | 2 |
Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin. Bertini, I., Calderone, V., Fragai, M. et al. J Med Chem (2009) 52:4838-4843. DOI 10.1021/jm900610k · PubMed
Other PDB entries of the same protein (UniProt P53041 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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