2wtt

Structure of the human p73 tetramerization domain (crystal form II)

Method: X-RAY DIFFRACTION

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1. Protein Identity and Related Structures Protein Identity & Related Structures

TUMOR PROTEIN P73

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 4	water × 4	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 4	water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P73_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–51； UniProt 351–399 Author chain B； PDBConstruct 3–51； UniProt 351–399 Author chain C； PDBConstruct 3–51； UniProt 351–399 Author chain D； PDBConstruct 3–51； UniProt 351–399 Author chain E； PDBConstruct 3–51； UniProt 351–399 Author chain F； PDBConstruct 3–51； UniProt 351–399 Author chain G； PDBConstruct 3–51； UniProt 351–399 Author chain H； PDBConstruct 3–51； UniProt 351–399 Author chain I； PDBConstruct 3–51； UniProt 351–399 Author chain J； PDBConstruct 3–51； UniProt 351–399 Author chain K； PDBConstruct 3–51； UniProt 351–399 Author chain L； PDBConstruct 3–51； UniProt 351–399 Author chain M； PDBConstruct 3–51； UniProt 351–399 Author chain N； PDBConstruct 3–51； UniProt 351–399 Author chain O； PDBConstruct 3–51； UniProt 351–399 Author chain P； PDBConstruct 3–51； UniProt 351–399

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2wtt
Deposition date deposition_date	2009-09-21
Structure title title	Structure of the human p73 tetramerization domain (crystal form II)
Keywords keywords	;ALTERNATIVE SPLICING, OLIGOMERIZATION DOMAIN, CELL-CYCLE CONTROL, TRANSCRIPTION FACTOR, COOPERATIVITY, PHOSPHOPROTEIN, UBL CONJUGATION, ACTIVATOR, TUMOR SUPPRESSION, DEVELOPMENT, TRANSCRIPTION, APOPTOSIS, CELL CYCLE, DNA BINDING, TRANSCRIPTION REGULATION ;; TRANSCRIPTION
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

2wtt__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2wtt__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wtt__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	17.79 Å
Rg (electron density)	16.76 Å
Total Rg	17.54 Å
Atom count	1490
Residues	169
Excluded volume	26884 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wtt__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2wtt__assembly_2__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2wtt__assembly_3__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2wtt__assembly_4__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (2)

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6. Fold Classification (SCOP + CATH) 29 domains

SCOP 2.08 (15 domains)

Domain ID domain_id	d2wtta_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttb_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttc_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttd_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wtte_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttf_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttg_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wtth_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wtti_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttj_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttk_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttl_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttn_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wtto_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

Domain ID domain_id	d2wttp_
Class class	a — All alpha proteins
Fold Fold fold	a.53 — p53 tetramerization domain
Superfamily Superfamily superfamily	a.53.1 — p53 tetramerization domain
Family Family family	a.53.1.0 — automated matches

CATH v4.4 (14 domains)

Domain ID domain_id	2wttA00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttB00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttC00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttD00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttE00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttF00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttG00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttH00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttI00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttJ00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttK00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttL00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttN00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

Domain ID domain_id	2wttP00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	170 — p53, subunit A
Homologous superfamily homologous superfamily	10 — p53-like tetramerisation domain

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Unit-cell length a length_a	56.120 Å
Unit-cell length b length_b	84.000 Å
Unit-cell length c length_c	169.790 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	64

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.300 Å
Low-resolution limit resolution_low	24.786 Å
R factor r_factor	0.2333
R_work r_work	0.2304
R_free r_free	0.2874

Description description	TUMOR PROTEIN P73
Molecular weight formula_weight	6225.7 kDa
Source method src_method	man
Copy count entity_count	16

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P
Atom count atom_count	5778

Structure of the human p73 tetramerization domain (crystal form II)

1. Protein Identity and Related Structures Protein Identity & Related Structures

TUMOR PROTEIN P73

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2wtt__assembly_1__model_1

2wtt__assembly_1__model_1 | I(q)

2wtt__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 29 domains

SCOP 2.08 (15 domains)

CATH v4.4 (14 domains)

7. Citations (1)

Source organism organism	HOMO SAPIENS
Common name common_name	HUMAN
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	ESCHERICHIA COLI

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	107

Structure of the human p73 tetramerization domain (crystal form II)

1. Protein Identity and Related Structures Protein Identity & Related Structures

TUMOR PROTEIN P73

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

2wtt__assembly_1__model_1

2wtt__assembly_1__model_1 | I(q)

2wtt__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 water

6. Fold Classification (SCOP + CATH) 29 domains

SCOP 2.08 (15 domains)

CATH v4.4 (14 domains)

7. Citations (1)