1jh4

Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip1

Method: SOLUTION NMR Dmax: 46.4 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-1 × 1 (Q9H074) 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; 3mM 15N-labeled 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 | 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 NMR sample composition:3mM unlabeled PABC; 3mM N15-labeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% 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-1

Homo sapiens

UniProt Q9H074

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 124–145 Fragment:22-residue fragment 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; 3mM 15N-labeled 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 | 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 NMR sample composition:3mM unlabeled PABC; 3mM N15-labeled peptide; 50mM phosphate buffer; 0.1M NaCl; 1mM NaN3; pH 6.3 | 90% H2O/10% 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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PAIP1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–22; UniProt 124–145

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 1jh4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jh4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1jh4
Deposition date deposition_date2001-06-27
Structure title titleSolution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip1
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_guinier17.21
Radius of gyration Rg (electron density) rg_electron17.26
Forward intensity I(0) i01994230000.00
Molecular weight molecular_weight382850.0 kDa
Excluded volume excluded_volume481520 ų
Envelope volume envelope_volume87652 ų
Hydration-shell volume shell_volume27671 ų
Envelope diameter envelope_diameter85.8
Shell Rg shell_rg33.46
Envelope Rg envelope_rg28.84
Shape Rg shape_rg17.25
Total Rg total_rg17.65
Total atoms total_atoms54120
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 dmax46.4
Rg (real space) rg_real15.86
Rg uncertainty (real space) rg_real_error0.10
I(0) (real space) i0_real1.8950e+09
I(0) uncertainty (real space) i0_real_error1.6770e+07
Rg (reciprocal space) rg_reciprocal17.50
I(0) (reciprocal space) i0_reciprocal1994000000.0000
Solution quality estimate total_estimate0.6814
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.1
Skewness Skewness skewness0.399
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.4600 −1
Current regularization parameter α current_alpha2.8600
Highest regularization parameter α highest_alpha266800.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.009; Oscil: 0.972; Stabil: 0.986; Sysdev: 0.000; Positv: 1.000; Valcen: 0.987; 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_idd1jh4a1
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_idd1jh4a2
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_id1jh4A01
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)