6tvm

LEDGF/p75 dimer (residues 345-467)

Method: SOLUTION NMR Dmax: 81.3 Å Quality: GOOD

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

PC4 and SFRS1-interacting protein

Homo sapiens

UniProt O75475

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 345–467 Chain B; UniProt 345–467 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120;Pressure 1 NMR sample composition:0.5 mM [U-13C; U-15N] LEDGF, 20 mM HEPES, 100 mM sodium chloride, 1 mM TCEP, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

34 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSIP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–128; UniProt 345–467 Author chain B; PDBConstruct 6–128; UniProt 345–467

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 6tvm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6tvm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6tvm
Deposition date deposition_date2020-01-10
Structure title titleLEDGF/p75 dimer (residues 345-467)
Keywords keywordsepigenetic reader, integrase-binding domain, domain-swapped dimer, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier22.51
Radius of gyration Rg (electron density) rg_electron22.17
Forward intensity I(0) i011281600000.00
Molecular weight molecular_weight876530.0 kDa
Excluded volume excluded_volume1090300 ų
Envelope volume envelope_volume144480 ų
Hydration-shell volume shell_volume40604 ų
Envelope diameter envelope_diameter91.8
Shell Rg shell_rg37.34
Envelope Rg envelope_rg28.89
Shape Rg shape_rg22.15
Total Rg total_rg22.45
Total atoms total_atoms124560
Residues n_residues7680
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 dmax81.3
Rg (real space) rg_real22.55
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.1280e+10
I(0) uncertainty (real space) i0_real_error1.5540e+08
Rg (reciprocal space) rg_reciprocal22.54
I(0) (reciprocal space) i0_reciprocal11280000000.0000
Solution quality estimate total_estimate0.7723
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.388
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6005000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.722; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.872; 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)