7mnp

Crystal Structure of the ZnF2 of Nucleoporin NUP358/RanBP2 in complex with Ran-GDP

Method: X-RAY DIFFRACTION Dmax: 82.6 Å Quality: GOOD

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

GTP-binding nuclear protein Ran

Homo sapiens

UniProt P62826

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 1–216 Mutation:F35S E3 SUMO-protein ligase RanBP2 × 1 (P49792) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;294 K;17 % (w/v) PEG 3,350; 0.1M Bis-Tris Resolution 2.05 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–216 Mutation:F35S E3 SUMO-protein ligase RanBP2 × 1 (P49792) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;294 K;17 % (w/v) PEG 3,350; 0.1M Bis-Tris Resolution 2.05 Å R-free 0.231

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.

137 other PDB entries and 202 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–217; UniProt 1–216 Author chain C; PDBConstruct 2–217; UniProt 1–216

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1407–1443 Not recorded GTP-binding nuclear protein Ran × 1 (P62826) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;294 K;17 % (w/v) PEG 3,350; 0.1M Bis-Tris Resolution 2.05 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1407–1443 Not recorded GTP-binding nuclear protein Ran × 1 (P62826) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;294 K;17 % (w/v) PEG 3,350; 0.1M Bis-Tris Resolution 2.05 Å R-free 0.231

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 2
Chains and sequence ranges Author chain B; PDBConstruct 6–42; UniProt 1407–1443 Author chain D; PDBConstruct 6–42; UniProt 1407–1443

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 7mnp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7mnp
Deposition date deposition_date2021-05-01
Structure title titleCrystal Structure of the ZnF2 of Nucleoporin NUP358/RanBP2 in complex with Ran-GDP
Keywords keywordsNUCLEAR PORE COMPLEX COMPONENT, NUCLEOCYTOPLASMIC TRANSPORT, TRANSPORT PROTEIN, ZINC FINGER; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.48
Radius of gyration Rg (electron density) rg_electron24.60
Forward intensity I(0) i050801600.00
Molecular weight molecular_weight55305.0 kDa
Excluded volume excluded_volume69298 ų
Envelope volume envelope_volume83540 ų
Hydration-shell volume shell_volume28399 ų
Envelope diameter envelope_diameter87.8
Shell Rg shell_rg31.79
Envelope Rg envelope_rg24.66
Shape Rg shape_rg24.60
Total Rg total_rg25.42
Total atoms total_atoms7750
Residues n_residues480
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 dmax82.6
Rg (real space) rg_real25.45
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real5.0800e+07
I(0) uncertainty (real space) i0_real_error7.4390e+05
Rg (reciprocal space) rg_reciprocal25.46
I(0) (reciprocal space) i0_reciprocal50800000.0000
Solution quality estimate total_estimate0.8182
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary81.3
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.340
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7053000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)