5BZX: PDB entry 5BZX

Crystal structure of human phosphatase PTEN treated with a bisperoxovanadium complex. Determined by X-ray diffraction at 2.5 Å resolution. Released 7 Oct 2015.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 4
Atoms: 11,230
Mol. weight: 149.91 kDa
Ligands: VO4, TLA
Released: 7 Oct 2015

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

Secondary structure: helices and β-sheets

5BZX contains 56 α-helices and 80 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.

Chains A and C: 14 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	50-61	12
β-strand	65-69	5	2
α-helix	78-81	4
β-strand	85-87	3	2
α-helix	95-97	3
α-helix	98-100	3
α-helix	101-114	14
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	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

Chain B: 14 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	7
β-strand	23	1	7
β-strand	25-29	5	8
β-strand	32-35	4	8
β-strand	38-39	2	9
β-strand	48-49	2	9
α-helix	50-61	12
β-strand	65-69	5	8
α-helix	78-81	4
β-strand	85-87	3	8
α-helix	98-100	3
α-helix	101-114	14
β-strand	119-123	5	8
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	10
β-strand	207	1	11
β-strand	210	1	11
β-strand	213-219	7	12
β-strand	222-226	5	12
β-strand	233-235	3	10
β-strand	238-250	13	10
β-strand	252-260	9	12
α-helix	261-263	3
β-strand	267-276	10	12
α-helix	277-279	3
α-helix	283	1
α-helix	310	1
β-strand	316-321	6	10
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	10

Chain D: 14 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	18	1	19
β-strand	23	1	19
β-strand	25-29	5	20
β-strand	32-35	4	20
β-strand	39	1	21
β-strand	49	1	21
α-helix	50-61	12
β-strand	65-69	5	20
α-helix	78-81	4
β-strand	85-87	3	20
α-helix	98-100	3
α-helix	101-114	14
β-strand	119-123	5	20
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	22
β-strand	207	1	23
β-strand	210	1	23
β-strand	213-219	7	24
β-strand	222-226	5	24
α-helix	227-228	2
β-strand	233-235	3	22
β-strand	238-250	13	22
β-strand	252-259	8	24
α-helix	267	1
β-strand	268-276	9	24
α-helix	277-279	3
α-helix	280-281	2
β-strand	316-321	6	22
α-helix	322-324	3
α-helix	328-330	3
β-strand	342-349	8	22

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

>5BZX_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
VO4	Vanadate ion	O4 V	2
TLA	L(+)-tartaric acid	C4 H6 O6	3

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
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
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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