4i9y

Structure of the C-terminal domain of Nup358

Method: X-RAY DIFFRACTION Dmax: 115.0 Å Quality: EXCELLENT

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 3062–3224 Not recorded GOL GLYCEROL × 3 CL CHLORIDE ION × 1 TLA L(+)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;294 K;0.1 M TRIS-HCL, 0.2 M NaCl, 0.9 M K/Na Tartrate, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.75 Å R-free 0.158
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3062–3224 Not recorded GOL GLYCEROL × 5 CL CHLORIDE ION × 1 TLA L(+)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;294 K;0.1 M TRIS-HCL, 0.2 M NaCl, 0.9 M K/Na Tartrate, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.75 Å R-free 0.158
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 3062–3224 Not recorded GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;294 K;0.1 M TRIS-HCL, 0.2 M NaCl, 0.9 M K/Na Tartrate, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.75 Å R-free 0.158
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 3062–3224 Not recorded GOL GLYCEROL × 5 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;294 K;0.1 M TRIS-HCL, 0.2 M NaCl, 0.9 M K/Na Tartrate, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.75 Å R-free 0.158
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 3062–3224 Not recorded GOL GLYCEROL × 2 CL CHLORIDE ION × 1 TLA L(+)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;294 K;0.1 M TRIS-HCL, 0.2 M NaCl, 0.9 M K/Na Tartrate, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.75 Å R-free 0.158
6 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain F; UniProt 3062–3224 Not recorded GOL GLYCEROL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.3;294 K;0.1 M TRIS-HCL, 0.2 M NaCl, 0.9 M K/Na Tartrate, pH 8.3, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 1.75 Å R-free 0.158

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 63 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 5–167; UniProt 3062–3224 Author chain B; PDBConstruct 5–167; UniProt 3062–3224 Author chain C; PDBConstruct 5–167; UniProt 3062–3224 Author chain D; PDBConstruct 5–167; UniProt 3062–3224 Author chain E; PDBConstruct 5–167; UniProt 3062–3224 Author chain F; PDBConstruct 5–167; UniProt 3062–3224

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 4i9y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4i9y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4i9y
Deposition date deposition_date2012-12-05
Structure title titleStructure of the C-terminal domain of Nup358
Keywords keywordsNuclear Pore Complex, 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_guinier36.53
Radius of gyration Rg (electron density) rg_electron36.05
Forward intensity I(0) i0203393000.00
Molecular weight molecular_weight112760.0 kDa
Excluded volume excluded_volume139920 ų
Envelope volume envelope_volume178090 ų
Hydration-shell volume shell_volume42075 ų
Envelope diameter envelope_diameter119.9
Shell Rg shell_rg41.75
Envelope Rg envelope_rg35.58
Shape Rg shape_rg36.02
Total Rg total_rg36.49
Total atoms total_atoms15652
Residues n_residues1002
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 dmax115.0
Rg (real space) rg_real36.50
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.0340e+08
I(0) uncertainty (real space) i0_real_error3.5610e+06
Rg (reciprocal space) rg_reciprocal36.52
I(0) (reciprocal space) i0_reciprocal203400000.0000
Solution quality estimate total_estimate0.9064
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.5
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.709
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33660000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd4i9ya1
Class classb — All beta proteins
Fold Fold foldb.62 — Cyclophilin-like
Superfamily Superfamily superfamilyb.62.1 — Cyclophilin-like
Family Family familyb.62.1.1 — Cyclophilin (peptidylprolyl isomerase)
Domain ID domain_idd4i9ya2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i9yb1
Class classb — All beta proteins
Fold Fold foldb.62 — Cyclophilin-like
Superfamily Superfamily superfamilyb.62.1 — Cyclophilin-like
Family Family familyb.62.1.1 — Cyclophilin (peptidylprolyl isomerase)
Domain ID domain_idd4i9yb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i9yc1
Class classb — All beta proteins
Fold Fold foldb.62 — Cyclophilin-like
Superfamily Superfamily superfamilyb.62.1 — Cyclophilin-like
Family Family familyb.62.1.1 — Cyclophilin (peptidylprolyl isomerase)
Domain ID domain_idd4i9yc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i9yd1
Class classb — All beta proteins
Fold Fold foldb.62 — Cyclophilin-like
Superfamily Superfamily superfamilyb.62.1 — Cyclophilin-like
Family Family familyb.62.1.1 — Cyclophilin (peptidylprolyl isomerase)
Domain ID domain_idd4i9yd2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i9ye1
Class classb — All beta proteins
Fold Fold foldb.62 — Cyclophilin-like
Superfamily Superfamily superfamilyb.62.1 — Cyclophilin-like
Family Family familyb.62.1.1 — Cyclophilin (peptidylprolyl isomerase)
Domain ID domain_idd4i9ye2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4i9yf1
Class classb — All beta proteins
Fold Fold foldb.62 — Cyclophilin-like
Superfamily Superfamily superfamilyb.62.1 — Cyclophilin-like
Family Family familyb.62.1.1 — Cyclophilin (peptidylprolyl isomerase)
Domain ID domain_idd4i9yf2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (6 domains)

Domain ID domain_id4i9yA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology100 — Cyclophilin
Homologous superfamily homologous superfamily10 — Cyclophilin-like
Domain ID domain_id4i9yB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology100 — Cyclophilin
Homologous superfamily homologous superfamily10 — Cyclophilin-like
Domain ID domain_id4i9yC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology100 — Cyclophilin
Homologous superfamily homologous superfamily10 — Cyclophilin-like
Domain ID domain_id4i9yD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology100 — Cyclophilin
Homologous superfamily homologous superfamily10 — Cyclophilin-like
Domain ID domain_id4i9yE00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology100 — Cyclophilin
Homologous superfamily homologous superfamily10 — Cyclophilin-like
Domain ID domain_id4i9yF00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology100 — Cyclophilin
Homologous superfamily homologous superfamily10 — Cyclophilin-like

8. Citations (1)

9. Files and Curves (10)