8srr

Cryo-EM structure of the CBC-ALYREF complex

Method: ELECTRON MICROSCOPY Dmax: 101.2 Å Quality: GOOD

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

Nuclear cap-binding protein subunit 1

Homo sapiens

UniProt Q09161

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–790 Not recorded Nuclear cap-binding protein subunit 2 × 1 (P52298) RNA and export factor binding protein 2 × 1 (Q4KL64) M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 Å

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.

17 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCBP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–790; UniProt 1–790

Nuclear cap-binding protein subunit 2

Homo sapiens

UniProt P52298

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–156 Not recorded Nuclear cap-binding protein subunit 1 × 1 (Q09161) RNA and export factor binding protein 2 × 1 (Q4KL64) M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 Å

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.

17 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCBP2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–156; UniProt 1–156

RNA and export factor binding protein 2

Mus musculus

UniProt Q4KL64

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–155 Not recorded Nuclear cap-binding protein subunit 1 × 1 (Q09161) Nuclear cap-binding protein subunit 2 × 1 (P52298) M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 Å

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 Q4KL64_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–160; UniProt 1–155

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 8srr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8srr
Deposition date deposition_date2023-05-06
Structure title titleCryo-EM structure of the CBC-ALYREF complex
Keywords keywordsmRNA nuclear export, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.39
Radius of gyration Rg (electron density) rg_electron31.21
Forward intensity I(0) i0198911000.00
Molecular weight molecular_weight113320.0 kDa
Excluded volume excluded_volume142190 ų
Envelope volume envelope_volume182810 ų
Hydration-shell volume shell_volume47439 ų
Envelope diameter envelope_diameter106.9
Shell Rg shell_rg39.37
Envelope Rg envelope_rg31.18
Shape Rg shape_rg31.20
Total Rg total_rg31.93
Total atoms total_atoms7975
Residues n_residues975
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 dmax101.2
Rg (real space) rg_real32.20
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.9890e+08
I(0) uncertainty (real space) i0_real_error3.2000e+06
Rg (reciprocal space) rg_reciprocal32.28
I(0) (reciprocal space) i0_reciprocal198900000.0000
Solution quality estimate total_estimate0.8923
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.3
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35600000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)