1D5R: PTEN Tumor Suppressor

Crystal Structure of the PTEN Tumor Suppressor. Determined by X-ray diffraction at 2.1 Å resolution. Released 4 Nov 1999.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,968
Mol. weight: 38.65 kDa
Ligands: TLA
Released: 4 Nov 1999

Explore 1D5R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1D5R 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
β-strand	18	1	1
β-strand	23	1	1
β-strand	25-29	5	2
β-strand	32-35	4	2
β-strand	39	1	3
β-strand	49	1	3
α-helix	50-60	11
β-strand	65-71	7	2
β-strand	85-90	6	2
α-helix	95-97	3
α-helix	98-110	13
α-helix	111-115	5
β-strand	119-123	5	2
α-helix	129-142	14
α-helix	148-159	12
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	252-259	8	6
α-helix	267	1
β-strand	268-276	9	6
α-helix	277-279	3
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
Phosphoinositide phosphatase pten	A	protein	324	Homo sapiens	P60484 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1D5R_1 PHOSPHOINOSITIDE PHOSPHATASE PTEN (chains A)
MIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYK
IYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKA
GKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHL
DYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQP
LPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEEVDNDKEYLVLTLTKNDLDKAN
KDKANRYFSPNFKVKLYFTKTVEE

Ligands and cofactors

ID	Name	Formula	Copies
TLA	L(+)-tartaric acid	C4 H6 O6	1

Primary citation

Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Lee, J.O., Yang, H., Georgescu, M.M. et al. Cell (1999) 99:323-334. DOI 10.1016/S0092-8674(00)81663-3 · 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
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…
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

About this viewer

MolViewer shows 1D5R directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.