9GFO: IASPP-CTD fusion to p63 peptide

iASPP-CTD fusion to p63 peptide. Determined by X-ray diffraction at 2.4 Å resolution. Released 18 Dec 2024.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,456
Mol. weight: 92.17 kDa
Released: 18 Dec 2024

Explore 9GFO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GFO contains 48 α-helices and 34 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 AAA and CCC: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	620-622	3
α-helix	627-637	11
α-helix	640-649	10
α-helix	663-669	7
α-helix	673-681	9
α-helix	696-702	7
α-helix	706-713	8
α-helix	731-733	3
α-helix	741-754	14
α-helix	759-761	3
β-strand	762-765	4	1
β-strand	769	1	2
β-strand	776	1	1
β-strand	779	1	2
β-strand	784-789	6	1
β-strand	798-803	6	1
β-strand	806-811	6	1
α-helix	812-814	3
β-strand	815-816	2	1
α-helix	819-821	3

Chain BBB: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	620-622	3
α-helix	627-637	11
α-helix	640-649	10
α-helix	663-669	7
α-helix	673-681	9
α-helix	696-702	7
α-helix	706-713	8
α-helix	731-733	3
α-helix	741-754	14
α-helix	759-761	3
β-strand	762-765	4	3
β-strand	769	1	4
β-strand	776	1	3
β-strand	779	1	4
β-strand	784-789	6	3
β-strand	792	1	5
β-strand	795	1	5
β-strand	798-803	6	3
β-strand	806-811	6	3
α-helix	812-814	3
β-strand	815-816	2	3
α-helix	819-821	3

Chain DDD: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	620-622	3
α-helix	627-637	11
α-helix	640-649	10
α-helix	663-669	7
α-helix	673-681	9
α-helix	696-702	7
α-helix	706-713	8
α-helix	730-733	4
α-helix	741-754	14
α-helix	758-761	4
β-strand	762-765	4	8
β-strand	769	1	9
β-strand	776	1	8
β-strand	779	1	9
β-strand	784-789	6	8
β-strand	798-803	6	8
β-strand	806-811	6	8
α-helix	812-814	3
β-strand	815-816	2	8
α-helix	819-823	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor protein 63,RelA-associated inhibitor	AAA, BBB, CCC, DDD	protein	210	Homo sapiens	Q8WUF5 (AlphaFold model), Q9H3D4 (AlphaFold model)

Sequence of entity 1 (AAA, BBB, CCC, DDD), FASTA

>9GFO_1 Tumor protein 63,RelA-associated inhibitor (chains AAA, BBB, CCC, DDD)
GTKRPFRQNLNPLVLLLDAALTGELEVVQQAVKEMNDPSQPNEEGITALHNAICGANYSI
VDFLITAGANVNSPDSHGWTPLHCAASCNDTVICMALVQHGAAIFATTLSDGATAFEKCD
PYREGYADCATYLADVEQSMGLMNSGAVYALWDYSAEFGDELSFREGESVTVLRRDGPEE
TDWWWAALHGQEGYVPRNYFGLFPRVKPQR

Primary citation

Alternative splicing in the DBD linker region of p63 modulates binding to DNA and iASPP in vitro. Lotz, R., Osterburg, C., Chaikuad, A. et al. Cell Death Dis (2025) 16:4-4. DOI 10.1038/s41419-024-07320-2 · PubMed

Other PDB entries of the same protein (UniProt Q8WUF5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6HL6 1.97 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and iASPP(670-693)
2VGE 2.1 Å, Crystal structure of the C-terminal region of human iASPP
6DCX 3.41 Å, iASPP-PP-1c structure and targeting of p53
6RZ3 4.23 Å, Crystal structure of a complex between the DNA-binding domain of p53 and the…

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