7JTX: PTEN regulation by multi-site phosphorylation

the structural basis of PTEN regulation by multi-site phosphorylation. Determined by X-ray diffraction at 3.23 Å resolution. Released 1 Sept 2021.

Method: X-ray diffraction
Resolution: 3.23 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,322
Mol. weight: 42.34 kDa
Released: 1 Sept 2021

Explore 7JTX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7JTX contains 10 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: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	26-29	4	1
β-strand	32-35	4	1
α-helix	51-60	10
β-strand	65-69	5	1
β-strand	84-87	4	1
α-helix	95-97	3
α-helix	98-100	3
α-helix	101-112	12
β-strand	119-123	5	1
α-helix	129-142	14
α-helix	148-158	11
α-helix	169-183	15
β-strand	192-200	9	2
β-strand	207	1	3
β-strand	210	1	3
β-strand	213-219	7	4
β-strand	222-226	5	4
β-strand	233-235	3	2
β-strand	238-250	13	2
β-strand	252-259	8	4
β-strand	268-276	9	4
α-helix	277-279	3
β-strand	316-321	6	2
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	A	protein	366	Homo sapiens	P60484 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7JTX_1 Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (chains A)
MEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHY
KIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCK
AGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNH
LDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQ
PLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEEDNDKEYLVLTLTKNDLDKAN
KDKANRYFSPNFKVKLYFTKTVEETGGGSGGTGGGSGGTGGGSGCYPSDPTPTDPSDPEN
EPFDED

Primary citation

The structural basis of PTEN regulation by multi-site phosphorylation. Dempsey, D.R., Viennet, T., Iwase, R. et al. Nat Struct Mol Biol (2021) 28:858-868. DOI 10.1038/s41594-021-00668-5 · PubMed

Other PDB entries of the same protein (UniProt P60484 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8X3S 1.87 Å, Crystal structure of human WDR5 in complex with PTEN
4O1V 2.0 Å, SPOP Promotes Tumorigenesis by Acting as a Key Regulatory Hub in Kidney Cancer
1D5R 2.1 Å, Crystal Structure of the PTEN Tumor Suppressor
7PC7 2.1 Å, The PDZ domain of SNTG1 complexed with the acetylated PDZ-binding motif of PTEN
5BZZ 2.2 Å, Crystal structure of human phosphatase PTEN in its reduced state
5BUG 2.4 Å, Crystal structure of human phosphatase PTEN oxidized by H2O2
5BZX 2.5 Å, Crystal structure of human phosphatase PTEN treated with a bisperoxovanadium complex
7JUL 2.53 Å, Crystal structure of non phosphorylated PTEN (n-crPTEN-13sp-T1, SDTTDSDPENEG)
7JUK 3.15 Å, Crystal structure of PTEN with a tetra-phosphorylated tail (4p-crPTEN-13sp-T2,…
7JVX 3.2 Å, Crystal structure of PTEN (aa 7-353 followed by spacer TGGGSGGTGGGSGGTGGGCY ligated to…
2KYL Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN
9A90 PTEN model. Model restrained with crosslinking-MS data from "strained" conformation and…

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