2x04

Crystal structure of the PABC-TNRC6C complex

Method: X-RAY DIFFRACTION Dmax: 60.9 Å Quality: GOOD

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 B; UniProt 456–530 Fragment:C-TERMINAL DOMAIN (PABC), RESIDUES 456-530 TRINUCLEOTIDE REPEAT-CONTAINING GENE 6C PROTEIN × 1 (Q9HCJ0) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;0.1 M NA-ACETATE PH 4.6, 200 MM AMMONIUM SULFATE, 30% (W/V) PEG 4000 Resolution 1.49 Å R-free 0.186
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 456–530 Fragment:C-TERMINAL DOMAIN (PABC), RESIDUES 456-530 TRINUCLEOTIDE REPEAT-CONTAINING GENE 6C PROTEIN × 1 (Q9HCJ0) X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;0.1 M NA-ACETATE PH 4.6, 200 MM AMMONIUM SULFATE, 30% (W/V) PEG 4000 Resolution 1.49 Å R-free 0.186

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 57 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 6–80; UniProt 456–530 Author chain B; PDBConstruct 6–80; UniProt 456–530

TRINUCLEOTIDE REPEAT-CONTAINING GENE 6C PROTEIN

OrganismNot specified

UniProt Q9HCJ0

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 D; UniProt 1382–1399 Fragment:DUF DOMAIN, RESIDUES 1382-1399 POLYADENYLATE-BINDING PROTEIN 1 × 1 (P11940) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;0.1 M NA-ACETATE PH 4.6, 200 MM AMMONIUM SULFATE, 30% (W/V) PEG 4000 Resolution 1.49 Å R-free 0.186
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1382–1399 Fragment:DUF DOMAIN, RESIDUES 1382-1399 POLYADENYLATE-BINDING PROTEIN 1 × 1 (P11940) X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;0.1 M NA-ACETATE PH 4.6, 200 MM AMMONIUM SULFATE, 30% (W/V) PEG 4000 Resolution 1.49 Å R-free 0.186

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNR6C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–18; UniProt 1382–1399 Author chain D; PDBConstruct 1–18; UniProt 1382–1399

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 2x04

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2x04
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2x04
Deposition date deposition_date2009-12-04
Structure title titleCrystal structure of the PABC-TNRC6C complex
Keywords keywords;PEPTIDE-RNA BINDING PROTEIN COMPLEX, RNA-MEDIATED GENE SILENCING, NUCLEUS, METHYLATION, SPLICEOSOME, TRANSLATION REGULATION, PROTEIN-PROTEIN COMPLEX, COILED COIL, DEADENYLATION, MRNA SPLICING, PHOSPHOPROTEIN, MRNA PROCESSING, MICRORNA SILENCING ;; PEPTIDE/RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.66
Radius of gyration Rg (electron density) rg_electron16.42
Forward intensity I(0) i07679180.00
Molecular weight molecular_weight20353.0 kDa
Excluded volume excluded_volume25584 ų
Envelope volume envelope_volume29557 ų
Hydration-shell volume shell_volume15258 ų
Envelope diameter envelope_diameter62.1
Shell Rg shell_rg22.06
Envelope Rg envelope_rg16.66
Shape Rg shape_rg16.39
Total Rg total_rg17.51
Total atoms total_atoms1424
Residues n_residues186
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 dmax60.9
Rg (real space) rg_real17.57
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real7.6790e+06
I(0) uncertainty (real space) i0_real_error9.4250e+04
Rg (reciprocal space) rg_reciprocal17.58
I(0) (reciprocal space) i0_reciprocal7679000.0000
Solution quality estimate total_estimate0.7810
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.350
Angular range angular_range— – 0.4500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1642000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.720; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2x04A01
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
Domain ID domain_id2x04B01
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)