4O1V: Speckle-type POZ protein

SPOP Promotes Tumorigenesis by Acting as a Key Regulatory Hub in Kidney Cancer. Determined by X-ray diffraction at 2.0 Å resolution. Released 30 Apr 2014.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,260
Mol. weight: 18.02 kDa
Released: 30 Apr 2014

Explore 4O1V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4O1V contains 5 α-helices and 13 β-strands across 2 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: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	29	1	1
β-strand	31-38	8	2
α-helix	41-43	3
β-strand	52-53	2	3
β-strand	57-59	3	3
β-strand	60	1	1
α-helix	61-63	3
β-strand	65-72	8	3
β-strand	83-92	10	3
β-strand	98-107	10	2
β-strand	113-118	6	2
β-strand	123-125	3	2
β-strand	130-138	9	3
α-helix	139-143	5
α-helix	145-147	3
α-helix	151-153	3
β-strand	155-165	11	2

Chain B: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	360	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Speckle-type POZ protein	A	protein	145	Homo sapiens	O43791 (AlphaFold model)
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN	B	protein	15	Homo sapiens	P60484 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4O1V_1 Speckle-type POZ protein (chains A)
GSGGSGKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESK
DYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDF
LLDEANGLLPDDKLTLFCEVSVVQD

Sequence of entity 2 (B), FASTA

>4O1V_2 Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (chains B)
PSNPEASSSTSVTPD

Primary citation

SPOP Promotes Tumorigenesis by Acting as a Key Regulatory Hub in Kidney Cancer. Li, G., Ci, W., Karmakar, S. et al. Cancer Cell (2014) 25:455-468. DOI 10.1016/j.ccr.2014.02.007 · PubMed

Other PDB entries of the same protein (UniProt O43791 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3IVV 1.25 Å, Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of…
7LIN 1.44 Å, X-ray structure of SPOP MATH domain (D140G) in complex with a 53BP1 peptide
7D3D 1.45 Å, Crystal structure of SPOP bound with a peptide
9HFV 1.45 Å, MyD88 peptide_2 bound to SPOP MATH domain
7LIP 1.48 Å, X-ray structure of SPOP MATH domain (D140G)
4HS2 1.53 Å, Crystal Structure of the Human SPOP C-terminal Domain
3HQL 1.66 Å, Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of…
3HQM 1.74 Å, Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of…
3IVB 1.75 Å, Structures of SPOP-Substrate Complexes: Insights into Architectures of BTB-Cul3…
6I5P 1.81 Å, Co-crystal structure of human SPOP MATH domain (E47K) and human BRD3 fragment
6I68 1.85 Å, Co-crystal structure of human SPOP MATH domain (M117V) and human BRD3 fragment
6I41 1.9 Å, Co-crystal structure of human SPOP MATH domain (wild-type) and human BRD3 fragment

Browse structure collections

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