1n52

Cap Binding Complex

Method: X-RAY DIFFRACTION Dmax: 100.0 Å Quality: GOOD

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

80 kDa nuclear cap binding protein

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 20 kDa nuclear cap binding protein × 1 (P52298) MG MAGNESIUM ION × 1 PG4 TETRAETHYLENE GLYCOL × 1 GOL GLYCEROL × 16 GTG 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.25;298 K;PEG 400, magnesium chloride, Tris, Glycine, Ethylene Glycol , pH 7.25, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.11 Å R-free 0.246

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 CB80_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–790; UniProt 1–790

20 kDa nuclear cap binding protein

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 80 kDa nuclear cap binding protein × 1 (Q09161) MG MAGNESIUM ION × 1 PG4 TETRAETHYLENE GLYCOL × 1 GOL GLYCEROL × 16 GTG 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.25;298 K;PEG 400, magnesium chloride, Tris, Glycine, Ethylene Glycol , pH 7.25, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.11 Å R-free 0.246

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 1n52

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1n52
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1n52
Deposition date deposition_date2002-11-04
Structure title titleCap Binding Complex
Keywords keywordsCBP80, CBP20, RNP domain, cap binding protein, m7GpppG, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.27
Radius of gyration Rg (electron density) rg_electron30.28
Forward intensity I(0) i0168709000.00
Molecular weight molecular_weight104740.0 kDa
Excluded volume excluded_volume131580 ų
Envelope volume envelope_volume161010 ų
Hydration-shell volume shell_volume43376 ų
Envelope diameter envelope_diameter106.7
Shell Rg shell_rg38.32
Envelope Rg envelope_rg30.22
Shape Rg shape_rg30.27
Total Rg total_rg30.98
Total atoms total_atoms7361
Residues n_residues880
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 dmax100.0
Rg (real space) rg_real31.16
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real1.6870e+08
I(0) uncertainty (real space) i0_real_error2.7120e+06
Rg (reciprocal space) rg_reciprocal31.21
I(0) (reciprocal space) i0_reciprocal168700000.0000
Solution quality estimate total_estimate0.8915
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.2
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31260000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.893

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1n52a1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.14 — MIF4G domain-like
Domain ID domain_idd1n52a2
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.14 — MIF4G domain-like
Domain ID domain_idd1n52a3
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.14 — MIF4G domain-like
Domain ID domain_idd1n52b_
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.58.7.1 — Canonical RBD

CATH v4.4 (4 domains)

Domain ID domain_id1n52A01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id1n52A02
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id1n52A03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily180
Domain ID domain_id1n52B00
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)