1hs5

NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CELLULAR TUMOR ANTIGEN P53

Homo sapiens

UniProt P04637

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 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 1–34; UniProt 324–357 Author chain B; PDBConstruct 1–34; UniProt 324–357

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_id1hs5
Deposition date deposition_date2000-12-22
Structure title titleNMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER
Keywords keywordsdimer, anti-parallel beta-turn-helix, GENE REGULATION; GENE REGULATION
Experimental Method methodSOLUTION NMR
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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.

1hs5__assembly_1__model_3

Assembly 1 · Model 3 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1hs5__assembly_1__model_3 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1hs5__assembly_1__model_3 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)14.33 Å
Rg (electron density)12.96 Å
Total Rg14.32 Å
Atom count1136
Residues68
Excluded volume10033 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1hs5__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1hs5__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1hs5__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1hs5__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1hs5__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1hs5__assembly_1__model_6 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1hs5__assembly_1__model_7 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1hs5__assembly_1__model_8 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1hs5__assembly_1__model_9 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1hs5__assembly_1__model_10 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 11 1hs5__assembly_1__model_11 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 12 1hs5__assembly_1__model_12 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 13 1hs5__assembly_1__model_13 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 14 1hs5__assembly_1__model_14 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 15 1hs5__assembly_1__model_15 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 16 1hs5__assembly_1__model_16 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 17 1hs5__assembly_1__model_17 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 18 1hs5__assembly_1__model_18 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 19 1hs5__assembly_1__model_19 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 20 1hs5__assembly_1__model_20 dimeric (2) 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 (1)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hs5a_
Class classa — All alpha proteins
Fold Fold folda.53 — p53 tetramerization domain
Superfamily Superfamily superfamilya.53.1 — p53 tetramerization domain
Family Family familya.53.1.1 — p53 tetramerization domain
Domain ID domain_idd1hs5b_
Class classa — All alpha proteins
Fold Fold folda.53 — p53 tetramerization domain
Superfamily Superfamily superfamilya.53.1 — p53 tetramerization domain
Family Family familya.53.1.1 — p53 tetramerization domain
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7. Citations (1)