8k00

RPA70N-MRE11 fusion

Method: X-RAY DIFFRACTION Dmax: 53.2 Å Quality: GOOD

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

Replication protein A 70 kDa DNA-binding subunit

Homo sapiens

UniProt P27694

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–120 Not recorded Double-strand break repair protein MRE11 × 1 (P49959) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;Ammonium sulate Resolution 1.40 Å R-free 0.199

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

41 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RFA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–121; UniProt 1–120

Double-strand break repair protein MRE11

Homo sapiens

UniProt P49959

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 538–563 Not recorded Replication protein A 70 kDa DNA-binding subunit × 1 (P27694) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;Ammonium sulate Resolution 1.40 Å R-free 0.199

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MRE11_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–31; UniProt 538–563

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.

SAXS scattering curve SAXS Profile

SAXS profile for 8k00

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k00
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k00
Deposition date deposition_date2023-07-07
Structure title titleRPA70N-MRE11 fusion
Keywords keywordsRPA, 70N, MRE11, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.20
Radius of gyration Rg (electron density) rg_electron14.75
Forward intensity I(0) i05351080.00
Molecular weight molecular_weight16232.0 kDa
Excluded volume excluded_volume20224 ų
Envelope volume envelope_volume23203 ų
Hydration-shell volume shell_volume13390 ų
Envelope diameter envelope_diameter52.1
Shell Rg shell_rg20.51
Envelope Rg envelope_rg15.02
Shape Rg shape_rg14.74
Total Rg total_rg15.88
Total atoms total_atoms1132
Residues n_residues151
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax53.2
Rg (real space) rg_real16.08
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real5.3510e+06
I(0) uncertainty (real space) i0_real_error5.9400e+04
Rg (reciprocal space) rg_reciprocal16.10
I(0) (reciprocal space) i0_reciprocal5351000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.108
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.4900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha964500.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8k00A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins

8. Citations (1)

9. Files and Curves (10)