2b29

N-terminal domain of the RPA70 subunit of human replication protein A.

Method: X-RAY DIFFRACTION Dmax: 52.6 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–120 Fragment:N-terminal domain (Residues 1-120) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;Ammonium Sulphate, Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.60 Å R-free 0.261

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 2b29

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2b29
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2b29
Deposition date deposition_date2005-09-18
Structure title titleN-terminal domain of the RPA70 subunit of human replication protein A.
Keywords keywordsREPLICATION; REPLICATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.15
Radius of gyration Rg (electron density) rg_electron13.56
Forward intensity I(0) i03335760.00
Molecular weight molecular_weight12856.0 kDa
Excluded volume excluded_volume16218 ų
Envelope volume envelope_volume18526 ų
Hydration-shell volume shell_volume11670 ų
Envelope diameter envelope_diameter48.9
Shell Rg shell_rg19.37
Envelope Rg envelope_rg13.99
Shape Rg shape_rg13.58
Total Rg total_rg14.83
Total atoms total_atoms899
Residues n_residues118
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 dmax52.6
Rg (real space) rg_real15.05
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real3.3360e+06
I(0) uncertainty (real space) i0_real_error4.0500e+04
Rg (reciprocal space) rg_reciprocal15.06
I(0) (reciprocal space) i0_reciprocal3336000.0000
Solution quality estimate total_estimate0.8542
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.157
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha637400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.701; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2b29a_
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

CATH v4.4 (1 domains)

Domain ID domain_id2b29A00
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)