4ga0

Structure of the N-terminal domain of Nup358

Method: X-RAY DIFFRACTION Dmax: 73.0 Å Quality: GOOD

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

E3 SUMO-protein ligase RanBP2

Homo sapiens

UniProt P49792

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 1–145 Fragment:unp residues 1-145 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277 K;18 % (w/v) PEG 3350 200 mM lithium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.15 Å R-free 0.239

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.

31 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–150; UniProt 1–145

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 4ga0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ga0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ga0
Deposition date deposition_date2012-07-24
Structure title titleStructure of the N-terminal domain of Nup358
Keywords keywordsTPR motif, Nuclear pore complex component Nucleocytoplasmic transport, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.19
Radius of gyration Rg (electron density) rg_electron18.41
Forward intensity I(0) i05102480.00
Molecular weight molecular_weight16631.0 kDa
Excluded volume excluded_volume20946 ų
Envelope volume envelope_volume24685 ų
Hydration-shell volume shell_volume12484 ų
Envelope diameter envelope_diameter73.3
Shell Rg shell_rg22.67
Envelope Rg envelope_rg18.96
Shape Rg shape_rg18.40
Total Rg total_rg19.21
Total atoms total_atoms2345
Residues n_residues143
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 dmax73.0
Rg (real space) rg_real19.43
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real5.1020e+06
I(0) uncertainty (real space) i0_real_error6.9210e+04
Rg (reciprocal space) rg_reciprocal19.39
I(0) (reciprocal space) i0_reciprocal5102000.0000
Solution quality estimate total_estimate0.7781
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.2
Skewness Skewness skewness0.630
Kurtosis Kurtosis kurtosis0.045
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha969500.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.569; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.416; Smooth: 0.988

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_id4ga0A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain

8. Citations (1)

9. Files and Curves (10)