6rx2

Fragment AZ-005 binding at the p53pT387/14-3-3 sigma interface

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

14-3-3 protein sigma

Homo sapiens

UniProt P31947

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Cellular tumor antigen p53 × 2 (P04637) MAGNESIUM ION × 6 CALCIUM ION × 2 7-[[(2~{S})-1-azanylpropan-2-yl]amino]-1-benzothiophene-2-carboximidamide × 2 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name 1433S_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–253; UniProt 1–248

Cellular tumor antigen p53

OrganismNot specified

UniProt P04637

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 14-3-3 protein sigma × 2 (P31947) MAGNESIUM ION × 6 CALCIUM ION × 2 7-[[(2~{S})-1-azanylpropan-2-yl]amino]-1-benzothiophene-2-carboximidamide × 2 water × 4 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 2
Chains and sequence ranges Author chain P; PDBConstruct 1–12; UniProt 382–393

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_id6rx2
Deposition date deposition_date2019-06-07
Structure title titleFragment AZ-005 binding at the p53pT387/14-3-3 sigma interface
Keywords keywordsprotein protein interaction, fragment soaking, stabilization, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-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.

6rx2__assembly_1__model_1

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

Download this curve (.dat)

6rx2__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6rx2__assembly_1__model_1 | 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)27.28 Å
Rg (electron density)26.32 Å
Total Rg27.05 Å
Atom count3664
Residues458
Excluded volume65061 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6rx2__assembly_1__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 (6)

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7. Citations (1)