7mnj

Crystal structure of the N-terminal domain of NUP358/RanBP2 (residues 145-673)

Method: X-RAY DIFFRACTION Dmax: 125.4 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 145–673 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;294 K;1% (w/v) PEG 2,000 MME; 0.8 M succinic acid; 0.1 M HEPES Resolution 3.80 Å R-free 0.242
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 145–673 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;294 K;1% (w/v) PEG 2,000 MME; 0.8 M succinic acid; 0.1 M HEPES Resolution 3.80 Å R-free 0.242
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 145–673 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;294 K;1% (w/v) PEG 2,000 MME; 0.8 M succinic acid; 0.1 M HEPES Resolution 3.80 Å R-free 0.242

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 66 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 1–529; UniProt 145–673 Author chain B; PDBConstruct 1–529; UniProt 145–673 Author chain C; PDBConstruct 1–529; UniProt 145–673

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 7mnj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mnj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mnj
Deposition date deposition_date2021-05-01
Structure title titleCrystal structure of the N-terminal domain of NUP358/RanBP2 (residues 145-673)
Keywords keywordsNUCLEAR PORE COMPLEX COMPONENT, NUCLEOCYTOPLASMIC TRANSPORT, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.30
Radius of gyration Rg (electron density) rg_electron37.70
Forward intensity I(0) i0484299000.00
Molecular weight molecular_weight180240.0 kDa
Excluded volume excluded_volume226190 ų
Envelope volume envelope_volume295860 ų
Hydration-shell volume shell_volume64101 ų
Envelope diameter envelope_diameter125.5
Shell Rg shell_rg44.65
Envelope Rg envelope_rg37.33
Shape Rg shape_rg37.71
Total Rg total_rg38.09
Total atoms total_atoms25365
Residues n_residues1586
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 dmax125.4
Rg (real space) rg_real38.17
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real4.8430e+08
I(0) uncertainty (real space) i0_real_error8.4930e+06
Rg (reciprocal space) rg_reciprocal38.25
I(0) (reciprocal space) i0_reciprocal484300000.0000
Solution quality estimate total_estimate0.8851
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.9
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.369
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha114500000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.908

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)