8smo

Crystal structure of the complex between truncated MLLE domain of PABPC1 and engineered superPAM2 peptide

Method: X-RAY DIFFRACTION Dmax: 94.4 Å Quality: EXCELLENT

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 556–626 Fragment:MLLE domain superPAM2 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
7 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain M; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292
8 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain O; UniProt 556–626 Fragment:MLLE domain superPAM2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;0.1 M citric acid pH 4.0, 1.6 M ammonium sulfate Resolution 3.00 Å R-free 0.292

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 51 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 6–76; UniProt 556–626 Author chain C; PDBConstruct 6–76; UniProt 556–626 Author chain E; PDBConstruct 6–76; UniProt 556–626 Author chain G; PDBConstruct 6–76; UniProt 556–626 Author chain I; PDBConstruct 6–76; UniProt 556–626 Author chain K; PDBConstruct 6–76; UniProt 556–626 Author chain M; PDBConstruct 6–76; UniProt 556–626 Author chain O; PDBConstruct 6–76; UniProt 556–626

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 8smo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8smo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8smo
Deposition date deposition_date2023-04-26
Structure title titleCrystal structure of the complex between truncated MLLE domain of PABPC1 and engineered superPAM2 peptide
Keywords keywordsMLLE domain, poly(A) binding protein, PAM2 motif, complex, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.05
Radius of gyration Rg (electron density) rg_electron31.12
Forward intensity I(0) i080918200.00
Molecular weight molecular_weight69545.0 kDa
Excluded volume excluded_volume86727 ų
Envelope volume envelope_volume130130 ų
Hydration-shell volume shell_volume34913 ų
Envelope diameter envelope_diameter92.7
Shell Rg shell_rg38.34
Envelope Rg envelope_rg29.96
Shape Rg shape_rg31.11
Total Rg total_rg31.91
Total atoms total_atoms4893
Residues n_residues710
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 dmax94.4
Rg (real space) rg_real31.79
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real8.0920e+07
I(0) uncertainty (real space) i0_real_error1.1120e+06
Rg (reciprocal space) rg_reciprocal31.91
I(0) (reciprocal space) i0_reciprocal80930000.0000
Solution quality estimate total_estimate0.9116
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.3
Skewness Skewness skewness-0.047
Kurtosis Kurtosis kurtosis-0.654
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7020000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)