2mke

Solution structure of CPEB1 ZZ domain in the free state

Method: SOLUTION NMR Dmax: 36.6 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytoplasmic polyadenylation element-binding protein 1

Homo sapiens

UniProt Q9BZB8

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 426–486 Fragment:UNP residues 426-486 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 0.15;Pressure ambient NMR sample composition:0.4-0.6 mM [U-100% 13C; U-100% 15N] CPEB1ZZ-1, 0.4-0.6 mM [U-100% 15N] CPEB1ZZ-2, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CPEB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–61; UniProt 426–486

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 2mke

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2mke
Deposition date deposition_date2014-02-06
Structure title titleSolution structure of CPEB1 ZZ domain in the free state
Keywords keywordsCPEB1, CPEB4, RRM, Cytoplasmic Polyadenylation Element, Translation regulation, TRANSLATION REGULATOR; TRANSLATION REGULATOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.44
Radius of gyration Rg (electron density) rg_electron13.27
Forward intensity I(0) i0669265000.00
Molecular weight molecular_weight195190.0 kDa
Excluded volume excluded_volume233920 ų
Envelope volume envelope_volume42885 ų
Hydration-shell volume shell_volume18605 ų
Envelope diameter envelope_diameter62.3
Shell Rg shell_rg25.84
Envelope Rg envelope_rg20.23
Shape Rg shape_rg13.29
Total Rg total_rg13.53
Total atoms total_atoms25662
Residues n_residues1586
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 dmax36.6
Rg (real space) rg_real12.79
Rg uncertainty (real space) rg_real_error0.06
I(0) (real space) i0_real6.4150e+08
I(0) uncertainty (real space) i0_real_error5.0600e+06
Rg (reciprocal space) rg_reciprocal13.58
I(0) (reciprocal space) i0_reciprocal669300000.0000
Solution quality estimate total_estimate0.6826
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary13.4
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha5.6630
Highest regularization parameter α highest_alpha97890.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.995; Stabil: 0.976; Sysdev: 0.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2mkeA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology640 — 30s Ribosomal Protein S18
Homologous superfamily homologous superfamily40 — Cytoplasmic polyadenylation element-binding protein, ZZ domain

8. Citations (1)

9. Files and Curves (10)