1YCS: P53-53BP2 complex

P53-53BP2 complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 19 Nov 1997.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,291
Mol. weight: 49.46 kDa
Ligands: ZN
Released: 19 Nov 1997

Explore 1YCS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YCS contains 16 α-helices and 20 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: 6 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	103	1	1
α-helix	105-107	3
β-strand	110-112	3	2
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	172-173	2
α-helix	177-181	5
β-strand	195-197	3	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	278-286	9

Chain B: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	328-337	10
α-helix	340-346	7
α-helix	363-370	8
α-helix	373-382	10
α-helix	396-402	7
α-helix	406-414	9
α-helix	430-433	4
α-helix	444-454	11
α-helix	459-461	3
β-strand	462-465	4	3
β-strand	469	1	4
β-strand	476	1	3
β-strand	479	1	4
β-strand	484-487	4	3
β-strand	498-503	6	3
β-strand	506-511	6	3
α-helix	512-514	3
β-strand	515-516	2	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
P53	A	protein	199	Homo sapiens	P04637 (AlphaFold model)
53BP2	B	protein	239	Homo sapiens	Q13625 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1YCS_1 P53 (chains A)
SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPP
GTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFR
HSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVR
VCACPGRDRRTEEENLRKK

Sequence of entity 2 (B), FASTA

>1YCS_2 53BP2 (chains B)
PEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLPLALLLDSSLEGEFDLVQRIIYEV
DDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCK
FLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYE
PQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Gorina, S., Pavletich, N.P. Science (1996) 274:1001-1005. DOI 10.1126/science.274.5289.1001 · 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

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