6emp

Solution structure of the LEDGF/p75 IBD - POGZ (aa 1370-1404) complex

Method: SOLUTION NMR Dmax: 62.2 Å Quality: REASONABLE

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

PC4 and SFRS1-interacting protein,Pogo transposable element with ZNF domain

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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 345–442 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 200;Pressure arbitraty NMR sample composition:0.5 mM [U-13C; U-15N] LEDGF/p75 IBD-POGZ, 50 mM TRIS, 150 mM sodium chloride, 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 7–104; UniProt 345–442

PC4 and SFRS1-interacting protein,Pogo transposable element with ZNF domain

Homo sapiens

UniProt Q7Z3K3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1326–1360 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 200;Pressure arbitraty NMR sample composition:0.5 mM [U-13C; U-15N] LEDGF/p75 IBD-POGZ, 50 mM TRIS, 150 mM sodium chloride, 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POGZ_HUMAN
Isoform Q7Z3K3-3
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 105–139; UniProt 1326–1360

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 6emp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6emp
Deposition date deposition_date2017-10-03
Structure title titleSolution structure of the LEDGF/p75 IBD - POGZ (aa 1370-1404) complex
Keywords keywordsprotein-protein complex, epigenetics, leukemia, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier16.74
Radius of gyration Rg (electron density) rg_electron16.37
Forward intensity I(0) i05974630000.00
Molecular weight molecular_weight640400.0 kDa
Excluded volume excluded_volume794360 ų
Envelope volume envelope_volume65512 ų
Hydration-shell volume shell_volume24779 ų
Envelope diameter envelope_diameter75.2
Shell Rg shell_rg29.28
Envelope Rg envelope_rg22.54
Shape Rg shape_rg16.38
Total Rg total_rg16.48
Total atoms total_atoms89320
Residues n_residues5560
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 dmax62.2
Rg (real space) rg_real16.73
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real5.9750e+09
I(0) uncertainty (real space) i0_real_error7.6560e+07
Rg (reciprocal space) rg_reciprocal16.73
I(0) (reciprocal space) i0_reciprocal5975000000.0000
Solution quality estimate total_estimate0.7390
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.062
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha828600.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.564; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.911; 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)