5e7n

Crystal Structure of RPA70N in complex with VU0085636

Method: X-RAY DIFFRACTION Dmax: 51.5 Å Quality: REASONABLE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–120 Fragment:residues 1-120 Mutation:E7R 5KR 2-({3-[(4-bromophenyl)sulfamoyl]-4-methylbenzoyl}amino)benzoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;294 K;100 mM MES, 200 mM Calcium Acetate, 20% PEG 8000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.21 Å R-free 0.215

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 4–123; UniProt 1–120

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 5e7n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5e7n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5e7n
Deposition date deposition_date2015-10-12
Structure title titleCrystal Structure of RPA70N in complex with VU0085636
Keywords keywordsInhibitor, Complex, PROTEIN BINDING-INHIBITOR complex; PROTEIN BINDING/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.38
Radius of gyration Rg (electron density) rg_electron13.88
Forward intensity I(0) i03958720.00
Molecular weight molecular_weight13975.0 kDa
Excluded volume excluded_volume17501 ų
Envelope volume envelope_volume19765 ų
Hydration-shell volume shell_volume12139 ų
Envelope diameter envelope_diameter53.2
Shell Rg shell_rg19.63
Envelope Rg envelope_rg14.28
Shape Rg shape_rg13.90
Total Rg total_rg15.04
Total atoms total_atoms1950
Residues n_residues123
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 dmax51.5
Rg (real space) rg_real15.29
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real3.9590e+06
I(0) uncertainty (real space) i0_real_error4.5600e+04
Rg (reciprocal space) rg_reciprocal15.30
I(0) (reciprocal space) i0_reciprocal3959000.0000
Solution quality estimate total_estimate0.6168
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha758200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.749; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5e7na1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.4 — Nucleic acid-binding proteins
Family Family familyb.40.4.3 — Single strand DNA-binding domain, SSB
Domain ID domain_idd5e7na2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id5e7nA00
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)