2n3a

Solution structure of LEDGF/p75 IBD in complex with POGZ peptide (1389-1404)

Method: SOLUTION NMR Dmax: 58.0 Å Quality: REASONABLE

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

Pogo transposable element with ZNF domain

OrganismNot specified

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1389–1404 Fragment:UNP residues 1389-1404 PC4 and SFRS1-interacting protein × 1 (O75475) SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 125;Pressure ambient NMR sample composition:0.5 mM peptide, 0.5 mM [U-13C; U-15N] protein, 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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–16; UniProt 1389–1404

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 348–426 Fragment:UNP residues 348-426 Pogo transposable element with ZNF domain × 1 (Q7Z3K3) SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 125;Pressure ambient NMR sample composition:0.5 mM peptide, 0.5 mM [U-13C; U-15N] protein, 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–79; UniProt 348–426

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 2n3a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2n3a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2n3a
Deposition date deposition_date2015-05-26
Structure title titleSolution structure of LEDGF/p75 IBD in complex with POGZ peptide (1389-1404)
Keywords keywordsLEDGF/p75, PogZ, H3K36me3, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.58
Radius of gyration Rg (electron density) rg_electron13.96
Forward intensity I(0) i01536750000.00
Molecular weight molecular_weight323720.0 kDa
Excluded volume excluded_volume402090 ų
Envelope volume envelope_volume41058 ų
Hydration-shell volume shell_volume18060 ų
Envelope diameter envelope_diameter64.2
Shell Rg shell_rg26.20
Envelope Rg envelope_rg20.73
Shape Rg shape_rg13.93
Total Rg total_rg14.26
Total atoms total_atoms45356
Residues n_residues2755
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 dmax58.0
Rg (real space) rg_real14.66
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.5370e+09
I(0) uncertainty (real space) i0_real_error2.0400e+07
Rg (reciprocal space) rg_reciprocal14.65
I(0) (reciprocal space) i0_reciprocal1537000000.0000
Solution quality estimate total_estimate0.7426
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.2
Skewness Skewness skewness0.605
Kurtosis Kurtosis kurtosis0.570
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha480800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.321; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.705; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2n3aB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology930 — Transcription Elongation Factor S-II; Chain A
Homologous superfamily homologous superfamily10 — Conserved domain common to transcription factors TFIIS, elongin A, CRSP70

8. Citations (1)

9. Files and Curves (10)