8c3j

Stapled peptide SP2 in complex with humanised RadA mutant HumRadA22

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

DNA repair and recombination protein RadA

Pyrococcus furiosus

UniProt O74036

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Breast cancer type 2 susceptibility protein × 1 (P51587) 2-[(4,6-diethyl-1,3,5-triazin-2-yl)-methyl-amino]ethanoic acid × 1 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 Breast cancer type 2 susceptibility protein × 1 (P51587) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name RADA_PYRFU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–231; UniProt 107–349 Author chain B; PDBConstruct 1–231; UniProt 107–349

Breast cancer type 2 susceptibility protein

Homo sapiens

UniProt P51587

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 DNA repair and recombination protein RadA × 1 (O74036) 2-[(4,6-diethyl-1,3,5-triazin-2-yl)-methyl-amino]ethanoic acid × 1 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 DNA repair and recombination protein RadA × 1 (O74036) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BRCA2_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–19; UniProt 1226–1244 Author chain C; PDBConstruct 22–36; UniProt 2050–2064 Author chain J; PDBConstruct 1–19; UniProt 1226–1244 Author chain J; PDBConstruct 22–36; UniProt 2050–2064

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_id8c3j
Deposition date deposition_date2022-12-26
Structure title titleStapled peptide SP2 in complex with humanised RadA mutant HumRadA22
Keywords keywordsStapled peptide, Rad51, BRCA2, BRC repeat, RECOMBINATION; RECOMBINATION
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.

8c3j__assembly_1__model_1

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

Download this curve (.dat)

8c3j__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.

8c3j__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)18.68 Å
Rg (electron density)17.34 Å
Total Rg18.41 Å
Atom count1855
Residues237
Excluded volume33036 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8c3j__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 8c3j__assembly_2__model_1 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 (3)

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7. Citations (1)