8gcj

PCNA

Method: X-RAY DIFFRACTION Dmax: 141.3 Å Quality: GOOD

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

Proliferating cell nuclear antigen

Homo sapiens

UniProt P12004

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–261 Chain C; UniProt 1–261 Chain E; UniProt 1–261 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.2 M Magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350 Resolution 2.85 Å R-free 0.278
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–261 Chain D; UniProt 1–261 Chain F; UniProt 1–261 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289.15 K;0.2 M Magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350 Resolution 2.85 Å R-free 0.278

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.

101 other PDB entries and 125 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCNA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–261; UniProt 1–261 Author chain B; PDBConstruct 1–261; UniProt 1–261 Author chain C; PDBConstruct 1–261; UniProt 1–261 Author chain D; PDBConstruct 1–261; UniProt 1–261 Author chain E; PDBConstruct 1–261; UniProt 1–261 Author chain F; PDBConstruct 1–261; UniProt 1–261

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 8gcj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8gcj
Deposition date deposition_date2023-03-01
Structure title titlePCNA
Keywords keywordsPCNA, DNA replication, replication; REPLICATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.79
Radius of gyration Rg (electron density) rg_electron42.10
Forward intensity I(0) i0381925000.00
Molecular weight molecular_weight158840.0 kDa
Excluded volume excluded_volume198690 ų
Envelope volume envelope_volume301220 ų
Hydration-shell volume shell_volume61076 ų
Envelope diameter envelope_diameter145.0
Shell Rg shell_rg46.25
Envelope Rg envelope_rg40.60
Shape Rg shape_rg42.10
Total Rg total_rg42.35
Total atoms total_atoms11146
Residues n_residues1514
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 dmax141.3
Rg (real space) rg_real42.74
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real3.8190e+08
I(0) uncertainty (real space) i0_real_error6.8270e+06
Rg (reciprocal space) rg_reciprocal42.79
I(0) (reciprocal space) i0_reciprocal381900000.0000
Solution quality estimate total_estimate0.8424
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.5
Skewness Skewness skewness0.311
Kurtosis Kurtosis kurtosis-0.215
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25590000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.703; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)