8ytc

PML-RBCC dimer

Method: ELECTRON MICROSCOPY Dmax: 74.2 Å Quality: GOOD

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

Protein PML

Homo sapiens

UniProt P29590

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 46–256 Chain B; UniProt 46–256 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.30 Å

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.

17 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PML_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–211; UniProt 46–256 Author chain B; PDBConstruct 1–211; UniProt 46–256

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 8ytc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ytc
Deposition date deposition_date2024-03-25
Structure title titlePML-RBCC dimer
Keywords keywordsPML nuclear body, RBCC dimer, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.06
Radius of gyration Rg (electron density) rg_electron21.54
Forward intensity I(0) i026662100.00
Molecular weight molecular_weight37489.0 kDa
Excluded volume excluded_volume46111 ų
Envelope volume envelope_volume57584 ų
Hydration-shell volume shell_volume22730 ų
Envelope diameter envelope_diameter78.1
Shell Rg shell_rg27.90
Envelope Rg envelope_rg21.35
Shape Rg shape_rg21.53
Total Rg total_rg22.38
Total atoms total_atoms2604
Residues n_residues332
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 dmax74.2
Rg (real space) rg_real22.03
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.6660e+07
I(0) uncertainty (real space) i0_real_error3.6720e+05
Rg (reciprocal space) rg_reciprocal22.03
I(0) (reciprocal space) i0_reciprocal26660000.0000
Solution quality estimate total_estimate0.7996
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.284
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7509000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)