5eay

Crystal structure of a Dna2 peptide in complex with Rpa 70N

Method: X-RAY DIFFRACTION Dmax: 86.7 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 3–120 Chain B; UniProt 3–120 Chain C; UniProt 3–120 Chain D; UniProt 3–120 Fragment:UNP residues 3-120 DNA replication ATP-dependent helicase/nuclease DNA2 × 4 (P51530) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;50 mM Tris-HCl, 35 % PEG 1500, 2 mM TCEP, pH 8.0 Resolution 1.55 Å R-free 0.267

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 1–118; UniProt 3–120 Author chain B; PDBConstruct 1–118; UniProt 3–120 Author chain C; PDBConstruct 1–118; UniProt 3–120 Author chain D; PDBConstruct 1–118; UniProt 3–120

DNA replication ATP-dependent helicase/nuclease DNA2

OrganismNot specified

UniProt P51530

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 5–17 Chain F; UniProt 5–17 Chain G; UniProt 5–17 Chain H; UniProt 5–17 Fragment:UNP residues 1-17 Replication protein A 70 kDa DNA-binding subunit × 4 (P27694) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;50 mM Tris-HCl, 35 % PEG 1500, 2 mM TCEP, pH 8.0 Resolution 1.55 Å R-free 0.267

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name DNA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–13; UniProt 5–17 Author chain F; PDBConstruct 1–13; UniProt 5–17 Author chain G; PDBConstruct 1–13; UniProt 5–17 Author chain H; PDBConstruct 1–13; UniProt 5–17

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 5eay

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5eay
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5eay
Deposition date deposition_date2015-10-17
Structure title titleCrystal structure of a Dna2 peptide in complex with Rpa 70N
Keywords keywordsDNA 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_guinier26.86
Radius of gyration Rg (electron density) rg_electron25.82
Forward intensity I(0) i049646000.00
Molecular weight molecular_weight56200.0 kDa
Excluded volume excluded_volume71257 ų
Envelope volume envelope_volume91738 ų
Hydration-shell volume shell_volume29517 ų
Envelope diameter envelope_diameter90.0
Shell Rg shell_rg33.26
Envelope Rg envelope_rg25.53
Shape Rg shape_rg25.81
Total Rg total_rg26.70
Total atoms total_atoms3933
Residues n_residues502
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 dmax86.7
Rg (real space) rg_real26.75
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.9650e+07
I(0) uncertainty (real space) i0_real_error6.6480e+05
Rg (reciprocal space) rg_reciprocal26.79
I(0) (reciprocal space) i0_reciprocal49650000.0000
Solution quality estimate total_estimate0.8994
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.2
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha22500000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5eayA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id5eayB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id5eayC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id5eayD00
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)