3pth

The PABC1 MLLE domain bound to the variant PAM2 motif of LARP4B

Method: X-RAY DIFFRACTION Dmax: 48.4 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 543–621 Fragment:UNP residues 543-621 La-related protein 4B × 1 (Q92615) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;289 K;2 ul protein solution at 43 mg/ml containing the 1.5 fold molar amount of peptide ligand was mixed with 2ul reservoir solution containing 1.5M magnesium sulfate, pH 6.5, VAPOR DIFFUSION, temperature 289K Resolution 1.70 Å R-free 0.218

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 4–82; UniProt 543–621

La-related protein 4B

OrganismNot specified

UniProt Q92615

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 55–69 Fragment:UNP residues 55-69 Polyadenylate-binding protein 1 × 1 (P11940) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6.5;289 K;2 ul protein solution at 43 mg/ml containing the 1.5 fold molar amount of peptide ligand was mixed with 2ul reservoir solution containing 1.5M magnesium sulfate, pH 6.5, VAPOR DIFFUSION, temperature 289K Resolution 1.70 Å R-free 0.218

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 LAR4B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 55–69

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 3pth

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3pth
Deposition date deposition_date2010-12-03
Structure title titleThe PABC1 MLLE domain bound to the variant PAM2 motif of LARP4B
Keywords keywordsMLLE domain, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.57
Radius of gyration Rg (electron density) rg_electron13.19
Forward intensity I(0) i02039910.00
Molecular weight molecular_weight9808.0 kDa
Excluded volume excluded_volume12337 ų
Envelope volume envelope_volume14402 ų
Hydration-shell volume shell_volume9731 ų
Envelope diameter envelope_diameter47.1
Shell Rg shell_rg18.35
Envelope Rg envelope_rg13.77
Shape Rg shape_rg13.21
Total Rg total_rg14.39
Total atoms total_atoms687
Residues n_residues90
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 dmax48.4
Rg (real space) rg_real14.54
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.0400e+06
I(0) uncertainty (real space) i0_real_error2.4620e+04
Rg (reciprocal space) rg_reciprocal14.54
I(0) (reciprocal space) i0_reciprocal2040000.0000
Solution quality estimate total_estimate0.8713
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.5
Skewness Skewness skewness0.279
Kurtosis Kurtosis kurtosis-0.185
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha306900.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id3pthA01
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)