6RZ3: Cellular tumor antigen p53

Crystal structure of a complex between the DNA-binding domain of p53 and the carboxyl-terminal conserved region of iASPP. Determined by X-ray diffraction at 4.23 Å resolution. Released 30 Oct 2019.

Method: X-ray diffraction
Resolution: 4.23 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,867
Mol. weight: 51.86 kDa
Ligands: ZN
Released: 30 Oct 2019

Explore 6RZ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6RZ3 contains 15 α-helices and 22 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: 7 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	92-94	3
β-strand	103	1	1
β-strand	110-113	4	2
β-strand	118	1	3
β-strand	121	1	3
β-strand	124-127	4	1
β-strand	132-135	4	1
β-strand	141-146	6	2
α-helix	150-152	3
β-strand	156-163	8	1
α-helix	166-168	3
α-helix	172-173	2
α-helix	177-181	5
β-strand	195-198	4	2
β-strand	204-207	4	1
β-strand	214-219	6	1
α-helix	222-224	3
β-strand	230-236	7	2
β-strand	251-258	8	1
β-strand	264-274	11	1
α-helix	278-289	12

Chain B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
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	4
β-strand	769	1	5
β-strand	776	1	4
β-strand	779	1	5
β-strand	784-789	6	4
β-strand	798-803	6	4
β-strand	806-811	6	4
α-helix	812-814	3
β-strand	815-816	2	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cellular tumor antigen p53	A	protein	232	Homo sapiens	P04637 (AlphaFold model)
RelA-associated inhibitor	B	protein	238	Homo sapiens	Q8WUF5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6RZ3_1 Cellular tumor antigen p53 (chains A)
MEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAK
SVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHE
RCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNS
SCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKK

Sequence of entity 2 (B), FASTA

>6RZ3_2 RelA-associated inhibitor (chains B)
MLNPLVLLLDAALTGELEVVQQAVKEMNDPSQPNEEGITALHNAICGANYSIVDFLITAG
ANVNSPDSHGWTPLHCAASCNDTVICMALVQHGAAIFATTLSDGATAFEKCDPYREGYAD
CATYLADVEQSMGLMNSGAVYALWDYSAEFGDELSFREGESVTVLRRDGPEETDWWWAAL
HGQEGYVPRNYFGLFPRVKPQRSKVLEGGSGGSGLNDIFEAQKIEWHEGRTKHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

iASPP mediates p53 selectivity through a modular mechanism fine-tuning DNA recognition. Chen, S., Wu, J., Zhong, S. et al. Proc Natl Acad Sci U S A (2019) 116:17470-17479. DOI 10.1073/pnas.1909393116 · PubMed

Other PDB entries of the same protein (UniProt P04637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9C5S 1.01 Å, Disulfide-linked, antiparallel p53-derived peptide dimer (CV1)
3D06 1.2 Å, Human p53 core domain with hot spot mutation R249S (I)
5MHC 1.2 Å, Crystal structure of 14-3-3sigma and a p53 C-terminal 12-mer synthetic phosphopeptide
8UQR 1.22 Å, Crystal structure of the human p53 tetramerization domain
6GGC 1.24 Å, p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9320
6SHZ 1.24 Å, p53 cancer mutant Y220C
4MZI 1.25 Å, Crystal structure of a human mutant p53
6GGE 1.25 Å, p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9327
3LW1 1.28 Å, Binary complex of 14-3-3 sigma and p53 pT387-peptide
5O1E 1.3 Å, p53 cancer mutant Y220C im complex with compound MB577
6RL3 1.3 Å, Fragment AZ-003 binding at the p53pT387/14-3-3 sigma interface
8E7A 1.3 Å, Crystal structure of the p53 (Y107H) core domain orthorhombic P form

Browse structure collections

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