4X34: 53BP1 tandem tudor domain

Crystal structure of the 53BP1 tandem tudor domain in complex with p53K381acK382me2. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Mar 2015.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,354
Mol. weight: 29.93 kDa
Released: 4 Mar 2015

Explore 4X34 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4X34 contains 9 α-helices and 24 β-strands across 3 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, 12 β-strands

Element	Residues	Length	Sheet
β-strand	1490-1494	5	1
β-strand	1501-1509	9	1
β-strand	1514-1519	6	1
β-strand	1524-1528	5	1
α-helix	1529-1531	3
β-strand	1532-1533	2	1
α-helix	1538-1539	2
β-strand	1543-1547	5	2
β-strand	1553-1564	12	2
β-strand	1567-1574	8	2
β-strand	1577-1582	6	2
α-helix	1583-1585	3
β-strand	1586-1587	2	2
β-strand	1588	1	1
α-helix	1590-1600	11
β-strand	1601	1	1

Chain B: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	1490-1494	5	3
β-strand	1501-1511	11	3
β-strand	1514-1519	6	3
β-strand	1524-1528	5	3
α-helix	1529-1531	3
β-strand	1532-1533	2	3
α-helix	1538-1539	2
β-strand	1543-1547	5	2
β-strand	1553-1564	12	2
β-strand	1567-1574	8	2
β-strand	1577-1582	6	2
α-helix	1583-1585	3
β-strand	1586-1587	2	2
β-strand	1588	1	3
α-helix	1590-1600	11
β-strand	1601	1	3

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	381-385	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor suppressor p53-binding protein 1	A, B	protein	120	Homo sapiens	Q12888 (AlphaFold model)
Thr-ser-arg-his-aly-mly-leu-met-phe-lys	C, D	protein	10	Homo sapiens	P04637 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4X34_1 Tumor suppressor p53-binding protein 1 (chains A, B)
NSFVGLRVVAKWSSNGYFYSGKITRDVGAGKYKLLFDDGYECDVLGKDILLCDPIPLDTE
VTALSEDEYFSAGVVKGHRKESGELYYSIEKEGQRKWYKRMAVILSLEQGNRLREQYGLG

Sequence of entity 2 (C, D), FASTA

>4X34_2 THR-SER-ARG-HIS-ALY-MLY-LEU-MET-PHE-LYS (chains C, D)
TSRHKKLMFK

Primary citation

An Acetyl-Methyl Switch Drives a Conformational Change in p53. Tong, Q., Mazur, S.J., Rincon-Arano, H. et al. Structure (2015) 23:322-331. DOI 10.1016/j.str.2014.12.010 · PubMed

Other PDB entries of the same protein (UniProt Q12888 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8SVI 1.15 Å, Ubiquitin variant i53:Mutant L67H with 53BP1 Tudor domain
8SVH 1.16 Å, Ubiquitin variant i53 mutant L67R bound to 53BP1 Tudor Domain
8SVG 1.21 Å, Ubiquitin variant i53 in complex with 53BP1 Tudor domain
2G3R 1.25 Å, Crystal Structure of 53BP1 tandem tudor domains at 1.2 A resolution
6VA5 1.28 Å, Tudor Domain of Tumor suppressor p53BP1 with MFP-4184
6VIP 1.36 Å, Tudor domain of tumor suppressor P53BP1 with mfp-6008
7LIN 1.44 Å, X-ray structure of SPOP MATH domain (D140G) in complex with a 53BP1 peptide
3LGF 1.5 Å, Crystal structure of the 53BP1 tandem tudor domain in complex with p53K370me2
4RG2 1.5 Å, Tudor Domain of Tumor suppressor p53BP1 with small molecule ligand
8SVJ 1.5 Å, Ubiquitin variant i53: mutant VHH with 53BP1 Tudor domain
8F0W 1.52 Å, Tudor Domain of Tumor suppressor p53BP1 with MFP-5956
3LGL 1.6 Å, Crystal structure of the 53BP1 tandem tudor domain in complex with p53K382me2

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