4f26

Crystal structure of the second RRM domain of human PABPC1 a pH 9.0

Method: X-RAY DIFFRACTION Dmax: 44.8 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 99–199 Fragment:RRM2 domain (un residues 99-119) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 9;294 K;25% PEG 1500 and 0.1 M MMT buffer , pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 2.00 Å R-free 0.286

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 6–106; UniProt 99–199

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 4f26

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4f26
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4f26
Deposition date deposition_date2012-05-07
Structure title titleCrystal structure of the second RRM domain of human PABPC1 a pH 9.0
Keywords keywordsRRM fold, translation initiation, RNA-binding, eIF4G-binding, sytoplasm, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.36
Radius of gyration Rg (electron density) rg_electron11.77
Forward intensity I(0) i01662880.00
Molecular weight molecular_weight8626.0 kDa
Excluded volume excluded_volume10789 ų
Envelope volume envelope_volume11876 ų
Hydration-shell volume shell_volume8872 ų
Envelope diameter envelope_diameter42.3
Shell Rg shell_rg17.10
Envelope Rg envelope_rg12.22
Shape Rg shape_rg11.74
Total Rg total_rg13.23
Total atoms total_atoms606
Residues n_residues77
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 dmax44.8
Rg (real space) rg_real13.31
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real1.6630e+06
I(0) uncertainty (real space) i0_real_error1.9130e+04
Rg (reciprocal space) rg_reciprocal13.31
I(0) (reciprocal space) i0_reciprocal1663000.0000
Solution quality estimate total_estimate0.8809
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.221
Kurtosis Kurtosis kurtosis-0.253
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha247600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.999

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_idd4f26a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id4f26A00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)