2rqh

Structure of GSPT1/ERF3A-PABC

Method: SOLUTION NMR Dmax: 57.4 Å Quality: GOOD

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

G1 to S phase transition 1

Mus musculus

UniProt Q8K2E1

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 24–45 Fragment:RESIDUES 73-94 (UNP residues 24-45) Polyadenylate-binding protein 1 × 1 (P11940) SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 0.15M;Pressure AMBIENT NMR sample composition:1 mM G1 TO S PHASE TRANSITION 1-1, 1 mM [U-98% 13C; U-98% 15N] POLYADENYLATE-BINDING PROTEIN 1-2, 93% H2O/7% D2O | 93% H2O/7% 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8K2E1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–22; UniProt 24–45

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 B; UniProt 541–623 Fragment:PABC DOMAIN G1 to S phase transition 1 × 1 (Q8K2E1) SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 0.15M;Pressure AMBIENT NMR sample composition:1 mM G1 TO S PHASE TRANSITION 1-1, 1 mM [U-98% 13C; U-98% 15N] POLYADENYLATE-BINDING PROTEIN 1-2, 93% H2O/7% D2O | 93% H2O/7% 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–83; UniProt 541–623

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 2rqh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2rqh
Deposition date deposition_date2009-05-08
Structure title titleStructure of GSPT1/ERF3A-PABC
Keywords keywords;PROTEIN-PROTEIN COMPLEX, GTP-binding, Nucleotide-binding, Alternative splicing, Cytoplasm, Methylation, mRNA processing, mRNA splicing, Nucleus, Phosphoprotein, RNA-binding, Spliceosome, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.01
Radius of gyration Rg (electron density) rg_electron14.63
Forward intensity I(0) i0689691000.00
Molecular weight molecular_weight226020.0 kDa
Excluded volume excluded_volume284890 ų
Envelope volume envelope_volume41563 ų
Hydration-shell volume shell_volume18532 ų
Envelope diameter envelope_diameter63.5
Shell Rg shell_rg25.12
Envelope Rg envelope_rg19.55
Shape Rg shape_rg14.63
Total Rg total_rg14.89
Total atoms total_atoms31980
Residues n_residues2100
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 dmax57.4
Rg (real space) rg_real15.02
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real6.8970e+08
I(0) uncertainty (real space) i0_real_error8.4330e+06
Rg (reciprocal space) rg_reciprocal15.02
I(0) (reciprocal space) i0_reciprocal689700000.0000
Solution quality estimate total_estimate0.7734
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis0.070
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha316400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.400; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.862; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2rqhb_
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

CATH v4.4 (1 domains)

Domain ID domain_id2rqhB01
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 (1)

9. Files and Curves (10)