SAXSdb — 1olg

▼

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

TUMOR SUPPRESSOR P53 (OLIGOMERIZATION DOMAIN)

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	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	P53_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–42； UniProt 319–360 Author chain B； PDBConstruct 1–42； UniProt 319–360 Author chain C； PDBConstruct 1–42； UniProt 319–360 Author chain D； PDBConstruct 1–42； UniProt 319–360

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1olg
Deposition date deposition_date	1994-06-13
Structure title title	HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR
Keywords keywords	ANTI-ONCOGENE; ANTI-ONCOGENE
Experimental Method method	SOLUTION NMR

▼

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.

1olg__assembly_1__model_1

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

Download this curve (.dat)

1olg__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1olg__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.98 Å
Rg (electron density)	19.18 Å
Total Rg	20.32 Å
Atom count	2792
Residues	168
Excluded volume	24715 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1olg__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1olga_
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.53.1.1 — p53 tetramerization domain

Domain ID domain_id	d1olgb_
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.53.1.1 — p53 tetramerization domain

Domain ID domain_id	d1olgc_
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.53.1.1 — p53 tetramerization domain

Domain ID domain_id	d1olgd_
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.53.1.1 — p53 tetramerization domain

CATH v4.4 (4 domains)

Domain ID domain_id	1olgA00
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	1olgB00
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	1olgC00
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	1olgD00
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

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	TUMOR SUPPRESSOR P53 (OLIGOMERIZATION DOMAIN)
Molecular weight formula_weight	4948.6 kDa
Source method src_method	man
Copy count entity_count	4

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	2792

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606

HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

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

TUMOR SUPPRESSOR P53 (OLIGOMERIZATION DOMAIN)

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

1olg__assembly_1__model_1

1olg__assembly_1__model_1 | I(q)

1olg__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

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

TUMOR SUPPRESSOR P53 (OLIGOMERIZATION DOMAIN)

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

1olg__assembly_1__model_1

1olg__assembly_1__model_1 | I(q)

1olg__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

5. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)