7mnn

Crystal structure of the N-terminal domain of NUP358/RanBP2 (residues 1-752) T653I mutant in complex with Fab fragment

Method: X-RAY DIFFRACTION Dmax: 190.8 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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–752 Mutation:I599M, T653I Antibody Fab14 Heavy Chain × 1 Antibody Fab14 Light Chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;294 K;4 (w/v) % PEG 4,000; 0.15 M sodium acetate; 0.1 M sodium citrate Resolution 6.70 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–752 Mutation:I599M, T653I Antibody Fab14 Heavy Chain × 1 Antibody Fab14 Light Chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;294 K;4 (w/v) % PEG 4,000; 0.15 M sodium acetate; 0.1 M sodium citrate Resolution 6.70 Å R-free 0.263

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 67 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 2–753; UniProt 1–752 Author chain B; PDBConstruct 2–753; UniProt 1–752

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 7mnn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mnn
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7mnn
Deposition date deposition_date2021-05-01
Structure title titleCrystal structure of the N-terminal domain of NUP358/RanBP2 (residues 1-752) T653I mutant in complex with Fab fragment
Keywords keywordsNUCLEAR PORE COMPLEX COMPONENT, NUCLEOCYTOPLASMIC TRANSPORT, TRANSPORT PROTEIN, TRANSPORT PROTEIN-Immune System complex; TRANSPORT PROTEIN/Immune System
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier59.15
Radius of gyration Rg (electron density) rg_electron59.75
Forward intensity I(0) i0885065000.00
Molecular weight molecular_weight248510.0 kDa
Excluded volume excluded_volume311220 ų
Envelope volume envelope_volume488970 ų
Hydration-shell volume shell_volume72703 ų
Envelope diameter envelope_diameter211.2
Shell Rg shell_rg54.79
Envelope Rg envelope_rg59.11
Shape Rg shape_rg59.76
Total Rg total_rg59.60
Total atoms total_atoms34833
Residues n_residues2233
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 dmax190.8
Rg (real space) rg_real59.68
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real8.8500e+08
I(0) uncertainty (real space) i0_real_error1.7230e+07
Rg (reciprocal space) rg_reciprocal58.67
I(0) (reciprocal space) i0_reciprocal883600000.0000
Solution quality estimate total_estimate0.8219
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary63.6
Skewness Skewness skewness0.472
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38960000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.882; Smooth: 0.052

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)