1jgn

Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip2

Method: SOLUTION NMR Dmax: 42.0 Å Quality: REASONABLE

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

polyadenylate-binding protein 1

Homo sapiens

UniProt P11940

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 544–636 Fragment:C-terminal domain polyadenylate-binding protein-interacting protein 2 × 1 (Q9BPZ3) SOLUTION NMR NMR measurement conditions:pH 6.3;303 K;Ionic strength (raw mmCIF value) 0.1M NaCl;Pressure ambient NMR sample composition:3mM 15N-labeled PABC; 4mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:3mM 15N,13C-labeled PABC; 4mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% D2O NMR sample composition:2.5mM 15N-labeled peptide; 3mM unlabeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:2mM 15N,13C-labeled peptide; 3mM unlabeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% D2O NMR sample composition:3mM unlabeled PABC; 3mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:3mM unlabeled PABC; 3mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% 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.

27 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PABP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–98; UniProt 544–636

polyadenylate-binding protein-interacting protein 2

Homo sapiens

UniProt Q9BPZ3

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 106–127 Fragment:C-terminal 22 residues polyadenylate-binding protein 1 × 1 (P11940) SOLUTION NMR NMR measurement conditions:pH 6.3;303 K;Ionic strength (raw mmCIF value) 0.1M NaCl;Pressure ambient NMR sample composition:3mM 15N-labeled PABC; 4mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:3mM 15N,13C-labeled PABC; 4mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% D2O NMR sample composition:2.5mM 15N-labeled peptide; 3mM unlabeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:2mM 15N,13C-labeled peptide; 3mM unlabeled PABC; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% D2O NMR sample composition:3mM unlabeled PABC; 3mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% D2O NMR sample composition:3mM unlabeled PABC; 3mM unlabeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 100% 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PAIP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–22; UniProt 106–127

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 1jgn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jgn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jgn
Deposition date deposition_date2001-06-26
Structure title titleSolution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip2
Keywords keywordsall-helical domain, protein-peptide complex, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.67
Radius of gyration Rg (electron density) rg_electron15.56
Forward intensity I(0) i01965930000.00
Molecular weight molecular_weight381740.0 kDa
Excluded volume excluded_volume481220 ų
Envelope volume envelope_volume65053 ų
Hydration-shell volume shell_volume23775 ų
Envelope diameter envelope_diameter73.2
Shell Rg shell_rg30.21
Envelope Rg envelope_rg24.50
Shape Rg shape_rg15.55
Total Rg total_rg15.89
Total atoms total_atoms54450
Residues n_residues3600
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 dmax42.0
Rg (real space) rg_real14.66
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real1.8680e+09
I(0) uncertainty (real space) i0_real_error1.5120e+07
Rg (reciprocal space) rg_reciprocal15.80
I(0) (reciprocal space) i0_reciprocal1966000000.0000
Solution quality estimate total_estimate0.6833
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.292
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha4.3980
Highest regularization parameter α highest_alpha230100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.979; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1jgna1
Class classa — All alpha proteins
Fold Fold folda.144 — PABP domain-like
Superfamily Superfamily superfamilya.144.1 — PABC (PABP) domain
Family Family familya.144.1.1 — PABC (PABP) domain
Domain ID domain_idd1jgna2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1jgnA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1900 — c-terminal domain of poly(a) binding protein
Homologous superfamily homologous superfamily10 — c-terminal domain of poly(a) binding protein

8. Citations (2)

9. Files and Curves (10)