7mnx

Crystal Structure of Nup358/RanBP2 Ran-binding domain 2 in complex with Ran-GPPNHP

Method: X-RAY DIFFRACTION Dmax: 149.5 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 Not recorded E3 SUMO-protein ligase RanBP2 × 1 (P49792) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–216 Not recorded E3 SUMO-protein ligase RanBP2 × 1 (P49792) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–216 Not recorded E3 SUMO-protein ligase RanBP2 × 1 (P49792) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–216 Not recorded E3 SUMO-protein ligase RanBP2 × 1 (P49792) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–216 Not recorded E3 SUMO-protein ligase RanBP2 × 1 (P49792) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 1–216 Not recorded E3 SUMO-protein ligase RanBP2 × 1 (P49792) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230

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 198 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 Author chain E; PDBConstruct 2–217; UniProt 1–216 Author chain G; PDBConstruct 2–217; UniProt 1–216 Author chain I; PDBConstruct 2–217; UniProt 1–216 Author chain K; 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 2012–2148 Fragment:RAN-binding domain 2 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2012-2148) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2012–2148 Fragment:RAN-binding domain 2 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2012-2148) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 2012–2148 Fragment:RAN-binding domain 2 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2012-2148) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 2012–2148 Fragment:RAN-binding domain 2 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2012-2148) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 2012–2148 Fragment:RAN-binding domain 2 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2012-2148) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 2012–2148 Fragment:RAN-binding domain 2 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2012-2148) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;294 K;15% w/v PEG3350, 0.125 M magnesium formate Resolution 2.40 Å R-free 0.230

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 2
Chains and sequence ranges Author chain B; PDBConstruct 5–141; UniProt 2012–2148 Author chain D; PDBConstruct 5–141; UniProt 2012–2148 Author chain F; PDBConstruct 5–141; UniProt 2012–2148 Author chain H; PDBConstruct 5–141; UniProt 2012–2148 Author chain J; PDBConstruct 5–141; UniProt 2012–2148 Author chain L; PDBConstruct 5–141; UniProt 2012–2148

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 7mnx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mnx
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7mnx
Deposition date deposition_date2021-05-01
Structure title titleCrystal Structure of Nup358/RanBP2 Ran-binding domain 2 in complex with Ran-GPPNHP
Keywords keywordsnuclear pore complex component, nucleocytoplasmic transport, TRANSPORT PROTEIN, complex (small GTPase-nuclear protein); TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.67
Radius of gyration Rg (electron density) rg_electron45.60
Forward intensity I(0) i0792584000.00
Molecular weight molecular_weight235220.0 kDa
Excluded volume excluded_volume295760 ų
Envelope volume envelope_volume411080 ų
Hydration-shell volume shell_volume76048 ų
Envelope diameter envelope_diameter160.6
Shell Rg shell_rg49.45
Envelope Rg envelope_rg44.75
Shape Rg shape_rg45.59
Total Rg total_rg45.80
Total atoms total_atoms33088
Residues n_residues2019
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 dmax149.5
Rg (real space) rg_real45.61
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real7.9260e+08
I(0) uncertainty (real space) i0_real_error1.3780e+07
Rg (reciprocal space) rg_reciprocal45.67
I(0) (reciprocal space) i0_reciprocal792600000.0000
Solution quality estimate total_estimate0.8809
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.5
Skewness Skewness skewness0.297
Kurtosis Kurtosis kurtosis-0.309
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47300000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.764

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)