5BZZ: Human phosphatase PTEN in its reduced state

Crystal structure of human phosphatase PTEN in its reduced state. Determined by X-ray diffraction at 2.2 Å resolution. Released 7 Oct 2015.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 11,268
Mol. weight: 149.83 kDa
Ligands: TLA
Released: 7 Oct 2015

Explore 5BZZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5BZZ contains 55 α-helices and 72 β-strands across 4 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: 14 helices, 18 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	50-61	12
β-strand	65-71	7	2
α-helix	78-80	3
β-strand	85-90	6	2
α-helix	95-97	3
α-helix	98-100	3
α-helix	101-112	12
β-strand	119-123	5	2
α-helix	129-141	13
α-helix	148-159	12
α-helix	169-183	15
α-helix	186-188	3
β-strand	192-200	9	4
β-strand	213-219	7	5
β-strand	222-226	5	5
α-helix	227-228	2
β-strand	233-235	3	4
β-strand	238-250	13	4
β-strand	252-259	8	5
α-helix	267	1
β-strand	268-276	9	5
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

Chain B: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	6
β-strand	23	1	6
β-strand	25-29	5	7
β-strand	32-35	4	7
β-strand	38-39	2	8
β-strand	48-49	2	8
α-helix	50-61	12
β-strand	65-71	7	7
α-helix	78-80	3
β-strand	85-90	6	7
α-helix	95-97	3
α-helix	98-100	3
α-helix	101-112	12
β-strand	119-123	5	7
α-helix	129-141	13
α-helix	148-159	12
α-helix	169-183	15
α-helix	186-188	3
β-strand	192-200	9	9
β-strand	213-219	7	10
β-strand	222-226	5	10
α-helix	227-228	2
β-strand	233-235	3	9
β-strand	238-250	13	9
β-strand	252-259	8	10
α-helix	266-267	2
β-strand	268-276	9	10
α-helix	277-279	3
β-strand	316-321	6	9
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	9

Chain C: 13 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	11
β-strand	23	1	11
β-strand	25-29	5	12
β-strand	32-35	4	12
β-strand	38-39	2	13
β-strand	48-49	2	13
α-helix	50-61	12
β-strand	65-71	7	12
α-helix	78-80	3
β-strand	85-90	6	12
α-helix	95-97	3
α-helix	98-112	15
β-strand	119-123	5	12
α-helix	129-141	13
α-helix	148-159	12
α-helix	169-183	15
α-helix	186-188	3
β-strand	192-200	9	14
β-strand	213-219	7	15
β-strand	222-226	5	15
α-helix	227-228	2
β-strand	233-235	3	14
β-strand	238-250	13	14
β-strand	252-259	8	15
α-helix	267	1
β-strand	268-276	9	15
α-helix	277-279	3
β-strand	316-321	6	14
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	14

Chain D: 14 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	16
β-strand	23	1	16
β-strand	25-29	5	17
β-strand	32-35	4	17
β-strand	39	1	18
β-strand	49	1	18
α-helix	50-61	12
β-strand	65-71	7	17
α-helix	78-80	3
β-strand	85-90	6	17
α-helix	95-97	3
α-helix	98-100	3
α-helix	101-112	12
β-strand	119-123	5	17
α-helix	129-141	13
α-helix	148-159	12
α-helix	169-184	16
α-helix	186-188	3
β-strand	192-200	9	19
β-strand	213-219	7	20
β-strand	222-226	5	20
α-helix	227-228	2
β-strand	233-235	3	19
β-strand	238-250	13	19
β-strand	252-259	8	20
α-helix	267	1
β-strand	268-276	9	20
α-helix	277-279	3
β-strand	316-321	6	19
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	A, B, C, D	protein	314	Homo sapiens	P60484 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5BZZ_1 Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (chains A, B, C, D)
RRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAE
RHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGV
MICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVAL
LFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDI
KVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEEDNDKEYLVLTLTKNDLDKANKDKANRYF
SPNFKVKLYFTKTV

Ligands and cofactors

ID	Name	Formula	Copies
TLA	L(+)-tartaric acid	C4 H6 O6	4

Primary citation

Redox Modulation of PTEN Phosphatase Activity by Hydrogen Peroxide and Bisperoxidovanadium Complexes. Lee, C.U., Hahne, G., Hanske, J. et al. Angew Chem Int Ed Engl (2015) 54:13796-13800. DOI 10.1002/anie.201506338 · 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
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…

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