6I7A: Speckle-type POZ protein

Co-crystal structure of human SPOP MATH domain (D140N) and human BRD3 fragment. Determined by X-ray diffraction at 2.2 Å resolution. Released 8 May 2019.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 8
Atoms: 4,676
Mol. weight: 70.2 kDa
Released: 8 May 2019

Explore 6I7A in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6I7A contains 20 α-helices and 44 β-strands across 8 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: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	30-38	9	1
α-helix	41-43	3
β-strand	52-53	2	2
β-strand	57	1	2
β-strand	67-72	6	2
β-strand	83-90	8	2
β-strand	98-107	10	1
β-strand	113-118	6	1
β-strand	123-125	3	1
β-strand	130-138	9	2
α-helix	139-143	5
α-helix	145-147	3
α-helix	151-153	3
β-strand	155-165	11	1

Chains B, D, F and H: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	247	1	2

Chain C: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	29-38	10	3
α-helix	41-43	3
β-strand	52-53	2	4
β-strand	57	1	4
β-strand	67-72	6	4
α-helix	78-80	3
β-strand	83-90	8	4
β-strand	99-107	9	3
β-strand	113-118	6	3
β-strand	123-124	2	3
β-strand	130-138	9	4
α-helix	139-142	4
α-helix	145-147	3
α-helix	151-153	3
β-strand	155-164	10	3

Chain E: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	30-38	9	1
α-helix	41-43	3
β-strand	52-53	2	5
α-helix	54-56	3
β-strand	57-58	2	5
β-strand	66-72	7	5
β-strand	83-90	8	5
β-strand	98-107	10	1
β-strand	113-118	6	1
β-strand	123-125	3	1
β-strand	130-138	9	5
α-helix	139-143	5
α-helix	145-147	3
α-helix	151-153	3
β-strand	155-165	11	1

Chain G: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	30-38	9	3
α-helix	41-43	3
β-strand	52-53	2	6
α-helix	54-56	3
β-strand	57-58	2	6
β-strand	66-72	7	6
β-strand	83-90	8	6
α-helix	93-94	2
β-strand	98-107	10	3
β-strand	113-118	6	3
β-strand	123-125	3	3
β-strand	130-138	9	6
α-helix	139-143	5
α-helix	145-147	3
α-helix	151-153	3
β-strand	155-163	9	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Speckle-type POZ protein	A, C, E, G	protein	145	Homo sapiens	O43791 (AlphaFold model)
Bromodomain-containing protein 3	B, D, F, H	protein	9	Homo sapiens	Q15059 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>6I7A_1 Speckle-type POZ protein (chains A, C, E, G)
GAMASGKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESK
DYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRNF
LLDEANGLLPDDKLTLFCEVSVVQD

Sequence of entity 2 (B, D, F, H), FASTA

>6I7A_2 Bromodomain-containing protein 3 (chains B, D, F, H)
KADTTTPTT

Primary citation

Structural Insights into BET Client Recognition of Endometrial and Prostate Cancer-Associated SPOP Mutants. Ostertag, M.S., Hutwelker, W., Plettenburg, O. et al. J Mol Biol (2019) 431:2213-2221. DOI 10.1016/j.jmb.2019.04.017 · 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

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