6trj

LEDGF/p75 IBD dimer

Method: X-RAY DIFFRACTION Dmax: 69.1 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 345–430 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;291 K;0.1M DL-Glutamic acid monohydrate; 0.1M DL-Alanine; 0.1M Glycine; 0.1M DL-Lysine monohydrochloride; 0.1M DL-Serine; 0.1 M Tris (base); BICINE pH 8.5; 20% v/v Glycerol; 10% w/v PEG 4000 (Morpheus Molecular Dimensions condition H11) Resolution 1.30 Å R-free 0.177

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 6–91; UniProt 345–430

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 6trj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6trj
Deposition date deposition_date2019-12-19
Structure title titleLEDGF/p75 IBD dimer
Keywords keywordsprotein-protein interaction, transcription factor, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.55
Radius of gyration Rg (electron density) rg_electron18.52
Forward intensity I(0) i02057380.00
Molecular weight molecular_weight9827.0 kDa
Excluded volume excluded_volume12324 ų
Envelope volume envelope_volume16878 ų
Hydration-shell volume shell_volume9186 ų
Envelope diameter envelope_diameter67.5
Shell Rg shell_rg21.45
Envelope Rg envelope_rg18.83
Shape Rg shape_rg18.48
Total Rg total_rg19.25
Total atoms total_atoms684
Residues n_residues85
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 dmax69.1
Rg (real space) rg_real18.87
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real2.0570e+06
I(0) uncertainty (real space) i0_real_error3.2190e+04
Rg (reciprocal space) rg_reciprocal18.82
I(0) (reciprocal space) i0_reciprocal2057000.0000
Solution quality estimate total_estimate0.7726
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.0
Skewness Skewness skewness0.637
Kurtosis Kurtosis kurtosis-0.156
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha147400.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.561; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.360; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6trja_
Class classa — All alpha proteins
Fold Fold folda.48 — N-cbl like
Superfamily Superfamily superfamilya.48.4 — HIV integrase-binding domain
Family Family familya.48.4.1 — HIV integrase-binding domain

8. Citations (1)

9. Files and Curves (10)