2WTT: Human p73 tetramerization domain

Structure of the human p73 tetramerization domain (crystal form II). Determined by X-ray diffraction at 2.3 Å resolution. Released 13 Oct 2009.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: HOMO SAPIENS
Chains: 16
Atoms: 5,778
Mol. weight: 99.61 kDa
Released: 13 Oct 2009

Explore 2WTT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WTT contains 44 α-helices and 16 β-strands across 16 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 A and B: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	354-360	7	1
α-helix	362-377	16
α-helix	378-380	3
α-helix	383-392	10

Chains C, D and L: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	354-360	7	2
α-helix	362-377	16
α-helix	378-380	3
α-helix	383-393	11

Chain E: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	354-359	6	3
α-helix	362-377	16
α-helix	378-380	3
α-helix	383-392	10

Chain F: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	355-360	6	3
α-helix	362-377	16
α-helix	378-380	3
α-helix	383-394	12

Chains G and I: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	354-359	6	4
α-helix	362-377	16
α-helix	378-380	3
α-helix	383-394	12

Chains H and J: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	355-360	6	4
α-helix	362-377	16
α-helix	378-380	3
α-helix	383-393	11

Chain K: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	354-360	7	6
α-helix	362-378	17
α-helix	383-393	11

Chain M: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	354-359	6	7
α-helix	362-377	16
α-helix	378-380	3

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tumor protein P73	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	protein	51	HOMO SAPIENS	O15350 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P), FASTA

>2WTT_1 TUMOR PROTEIN P73 (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P)
GSDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRP

Primary citation

Structural Evolution of P53, P63, and P73: Implication for Heterotetramer Formation. Joerger, A.C., Rajagopalan, S., Natan, E. et al. Proc Natl Acad Sci U S A (2009) 106:17705. DOI 10.1073/PNAS.0905867106 · PubMed

Other PDB entries of the same protein (UniProt O15350 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5HOB 1.22 Å, p73 homo-tetramerization domain mutant I
5HOC 1.36 Å, p73 homo-tetramerization domain mutant II
2WQI 1.7 Å, Crystal structure of the human p73 tetramerization domain
8P9C 1.76 Å, Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with…
9GNB 1.8 Å, Structure of p73 SAM domain in complex with DARPin B9
2XWC 1.82 Å, Crystal structure of the DNA binding domain of human TP73 refined at 1.8 A resolution
2WQJ 2.0 Å, Crystal structure of a truncated variant of the human p73 tetramerization domain
9GLQ 2.1 Å, Crystal structure of p73 tetramerisation domain in complex with darpins 1800
8P9E 2.25 Å, Crystal structure of wild type p63-p73 heterotetramer (tetramerisation domain) in…
4A63 2.27 Å, Crystal structure of the p73-ASPP2 complex at 2.6A resolution
1DXS 2.54 Å, Crystal structure of the C-terminal sterile alpha motif (SAM) domain of human p73 alpha…
8P9D 2.7 Å, Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with…

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