7JVX: PTEN

Crystal structure of PTEN (aa 7-353 followed by spacer TGGGSGGTGGGSGGTGGGCY ligated to peptide pSDpTpTDpSDPENEPFDED). Determined by X-ray diffraction at 3.2 Å resolution. Released 4 Aug 2021.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,639
Mol. weight: 48.75 kDa
Ligands: PO4
Released: 4 Aug 2021

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

Secondary structure: helices and β-sheets

7JVX contains 12 α-helices and 20 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: 12 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	8-11	4
β-strand	18	1	1
β-strand	21	1	1
β-strand	25-27	3	2
β-strand	32-36	5	2
α-helix	37-38	2
β-strand	39	1	3
β-strand	49	1	3
α-helix	50-60	11
β-strand	68-71	4	2
β-strand	86-90	5	2
α-helix	95-97	3
α-helix	98-114	17
β-strand	120-124	5	2
α-helix	129-142	14
α-helix	148-158	11
α-helix	169-184	16
β-strand	192-200	9	4
β-strand	207	1	5
β-strand	210	1	5
β-strand	213-219	7	6
β-strand	222-226	5	6
α-helix	227-228	2
β-strand	233-235	3	4
β-strand	238-250	13	4
β-strand	252-260	9	6
α-helix	261	1
β-strand	267-276	10	6
β-strand	316-321	6	4
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	A	protein	422	Homo sapiens	P60484 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7JVX_1 Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (chains A)
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSK
HKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVA
AIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSY
LLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMY
FEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEI
DSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEAS
SSTSVTPDVSDNEPDHYRYSTGGGSGGTGGGSGGTGGGCDTTDSDPENEPFDEDQHTQIT
KV

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2

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,…
7JTX 3.23 Å, the structural basis of PTEN regulation by multi-site phosphorylation
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…

Browse structure collections

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