8suy

Cryo-EM structure of the human cap binding complex (CBC)

Method: ELECTRON MICROSCOPY Dmax: 100.3 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–790 Not recorded 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 3.38 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–156 Not recorded Nuclear cap-binding protein subunit 1 × 1 (Q09161) M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.38 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

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 8suy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8suy
Deposition date deposition_date2023-05-14
Structure title titleCryo-EM structure of the human cap binding complex (CBC)
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_guinier31.99
Radius of gyration Rg (electron density) rg_electron30.87
Forward intensity I(0) i0169491000.00
Molecular weight molecular_weight104650.0 kDa
Excluded volume excluded_volume131360 ų
Envelope volume envelope_volume167530 ų
Hydration-shell volume shell_volume44427 ų
Envelope diameter envelope_diameter107.7
Shell Rg shell_rg38.70
Envelope Rg envelope_rg30.76
Shape Rg shape_rg30.87
Total Rg total_rg31.56
Total atoms total_atoms7366
Residues n_residues895
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 dmax100.3
Rg (real space) rg_real31.85
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.6950e+08
I(0) uncertainty (real space) i0_real_error2.6560e+06
Rg (reciprocal space) rg_reciprocal31.91
I(0) (reciprocal space) i0_reciprocal169500000.0000
Solution quality estimate total_estimate0.8925
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.365
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30640000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.850

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)