6ZK6: Protein Phosphatase 1 (PP1) T320E mutant

Protein Phosphatase 1 (PP1) T320E mutant. Determined by X-ray diffraction at 1.9 Å resolution. Released 18 Nov 2020.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
1
Atoms
2,434
Mol. weight
38.01 kDa
Ligands
FE, PO4, MN
Released
18 Nov 2020

Explore 6ZK6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ZK6 contains 14 α-helices and 16 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: 14 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix9-179
α-helix231
α-helix32-4817
β-strand52-5541
β-strand59-6242
β-strand6413
α-helix69-7911
β-strand87-8932
α-helix100-11314
β-strand118-12032
α-helix128-1347
α-helix136-1438
α-helix146-15611
β-strand162-16541
β-strand169-17131
α-helix183-1875
α-helix194-1963
α-helix200-2067
β-strand208-20924
β-strand216-21834
β-strand225-22734
α-helix229-23911
β-strand243-24641
β-strand255-25841
β-strand263-26641
β-strand26713
α-helix272-2743
α-helix278-2792
β-strand280-28562
β-strand291-29662

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunitAprotein331Homo sapiensP62136 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6ZK6_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A)
GMSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPL
KICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFF
LLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPD
LQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKH
DLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA
DKNKGKYGQFSGLNPGGRPIEPPRNSAKAKK

Ligands and cofactors

IDNameFormulaCopies
FEFE (III) ionFe2
PO4Phosphate ionO4 P1
MNManganese (II) ionMn2

Primary citation

Towards Dissecting the Mechanism of Protein Phosphatase-1 Inhibition by Its C-Terminal Phosphorylation. Salvi, F., Hoermann, B., Del Pino Garcia, J. et al. Chembiochem (2021) 22:834-838. DOI 10.1002/cbic.202000669 · PubMed

Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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