3H66: Serine/threonine-protein phosphatase 5

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms. Determined by X-ray diffraction at 2.59 Å resolution. Released 29 Sept 2009.

Method
X-ray diffraction
Resolution
2.59 Å
Organism
Homo sapiens
Chains
2
Atoms
5,116
Mol. weight
72.16 kDa
Ligands
ZN
Released
29 Sept 2009

Explore 3H66 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3H66 contains 27 α-helices and 33 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.

Chain A: 13 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix188-19912
α-helix206-22116
β-strand226-22941
β-strand236-24052
α-helix247-25711
β-strand26113
β-strand26413
β-strand266-26942
α-helix279-29214
β-strand297-30042
α-helix307-3137
α-helix315-3228
α-helix325-33511
β-strand341-34441
β-strand348-35031
α-helix363-3675
α-helix375-3762
α-helix380-3867
β-strand388-38924
β-strand395-39734
β-strand404-40634
α-helix408-41811
β-strand422-42541
β-strand43215
β-strand434-43741
α-helix438-4403
β-strand442-44541
α-helix451-4544
β-strand45815
β-strand459-46572
β-strand468-47692
Chain B: 14 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix188-19912
α-helix202-2054
α-helix206-22116
β-strand226-22946
β-strand236-24057
α-helix247-25711
β-strand266-26947
α-helix279-29214
β-strand297-30047
α-helix307-3137
α-helix315-3228
α-helix325-33511
β-strand341-34446
β-strand348-35146
α-helix363-3686
α-helix380-3867
β-strand388-38928
β-strand395-39738
β-strand404-40638
α-helix408-41811
β-strand422-42546
β-strand432-43327
β-strand434-43746
α-helix438-4403
β-strand442-44546
α-helix451-4544
β-strand458-46587
β-strand468-47697
α-helix478-4803

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase 5A, Bprotein315Homo sapiensP53041 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3H66_1 Serine/threonine-protein phosphatase 5 (chains A, B)
YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETE
KITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPD
HFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGL
FSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL
EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQ
FTAVPHPNVKPMAYA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

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:

Browse structure collections

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