8pnt

Structure of the human nuclear cap-binding complex bound to PHAX and m7G-capped RNA

Method: ELECTRON MICROSCOPY Dmax: 101.8 Å Quality: REASONABLE

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 20–790 Not recorded Nuclear cap-binding protein subunit 2 × 1 (P52298) Phosphorylated adapter RNA export protein × 2 (Q9H814) MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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 2–772; UniProt 20–790

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–156 Not recorded Nuclear cap-binding protein subunit 1 × 1 (Q09161) Phosphorylated adapter RNA export protein × 2 (Q9H814) MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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

Phosphorylated adapter RNA export protein

Homo sapiens

UniProt Q9H814

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–394 Chain D; UniProt 1–394 Not recorded Nuclear cap-binding protein subunit 1 × 1 (Q09161) Nuclear cap-binding protein subunit 2 × 1 (P52298) MGT 7N-METHYL-8-HYDROGUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHAX_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–394; UniProt 1–394 Author chain D; PDBConstruct 1–394; UniProt 1–394

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 8pnt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8pnt
Deposition date deposition_date2023-07-01
最后修订 last_revision2024-01-17
Structure title titleStructure of the human nuclear cap-binding complex bound to PHAX and m7G-capped RNA
Keywords keywordsNuclear cap-binding complex, PHAX, Pol II transcript metabolism, 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_guinier31.91
Radius of gyration Rg (electron density) rg_electron30.80
Forward intensity I(0) i0181317000.00
Molecular weight molecular_weight108130.0 kDa
Excluded volume excluded_volume135660 ų
Envelope volume envelope_volume174080 ų
Hydration-shell volume shell_volume45815 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg38.93
Envelope Rg envelope_rg30.82
Shape Rg shape_rg30.79
Total Rg total_rg31.53
Total atoms total_atoms15133
Residues n_residues927
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 dmax101.8
Rg (real space) rg_real31.76
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.8130e+08
I(0) uncertainty (real space) i0_real_error2.5310e+06
Rg (reciprocal space) rg_reciprocal31.82
I(0) (reciprocal space) i0_reciprocal181300000.0000
Solution quality estimate total_estimate0.6974
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.7
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36370000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 0.169; Positv: 1.000; Valcen: 0.989; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)