3kus

Crystal structure of the MLLE domain of poly(A)-binding protein in complex with the binding region of Paip2

Method: X-RAY DIFFRACTION Dmax: 65.0 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 A; UniProt 544–626 Fragment:C-terminal domain PAIP2 protein × 1 (Q6FID7) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;2.3M ammonium sulfate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.40 Å R-free 0.205
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 544–626 Fragment:C-terminal domain PAIP2 protein × 1 (Q6FID7) EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;2.3M ammonium sulfate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.40 Å R-free 0.205

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 6–88; UniProt 544–626 Author chain B; PDBConstruct 6–88; UniProt 544–626

PAIP2 protein

OrganismNot specified

UniProt Q6FID7

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 C; UniProt 109–123 Fragment:PABPC1-binding region Polyadenylate-binding protein 1 × 1 (P11940) GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;2.3M ammonium sulfate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.40 Å R-free 0.205
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 109–123 Fragment:PABPC1-binding region Polyadenylate-binding protein 1 × 1 (P11940) EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;2.3M ammonium sulfate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.40 Å R-free 0.205

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6FID7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–15; UniProt 109–123 Author chain D; PDBConstruct 1–15; UniProt 109–123

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 3kus

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3kus
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3kus
Deposition date deposition_date2009-11-27
Structure title titleCrystal structure of the MLLE domain of poly(A)-binding protein in complex with the binding region of Paip2
Keywords keywords;protein-protein complex, Methylation, mRNA processing, mRNA splicing, Nucleus, Phosphoprotein, RNA-binding, Spliceosome, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.95
Radius of gyration Rg (electron density) rg_electron17.83
Forward intensity I(0) i07119380.00
Molecular weight molecular_weight19519.0 kDa
Excluded volume excluded_volume24532 ų
Envelope volume envelope_volume29565 ų
Hydration-shell volume shell_volume14554 ų
Envelope diameter envelope_diameter63.7
Shell Rg shell_rg23.01
Envelope Rg envelope_rg18.36
Shape Rg shape_rg17.85
Total Rg total_rg18.69
Total atoms total_atoms1364
Residues n_residues177
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 dmax65.0
Rg (real space) rg_real18.94
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real7.1190e+06
I(0) uncertainty (real space) i0_real_error9.2460e+04
Rg (reciprocal space) rg_reciprocal18.94
I(0) (reciprocal space) i0_reciprocal7119000.0000
Solution quality estimate total_estimate0.8719
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.9
Skewness Skewness skewness0.317
Kurtosis Kurtosis kurtosis-0.364
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1369000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3kusA01
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_id3kusB01
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)