7mnz

Crystal Structure of Nup358/RanBP2 Ran-binding domain 4 in complex with Ran-GPPNHP

Method: X-RAY DIFFRACTION Dmax: 156.6 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 1–215 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–215 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–215 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–215 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–215 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 1–215 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225

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 2–216; UniProt 1–215 Author chain C; PDBConstruct 2–216; UniProt 1–215 Author chain E; PDBConstruct 2–216; UniProt 1–215 Author chain G; PDBConstruct 2–216; UniProt 1–215 Author chain I; PDBConstruct 2–216; UniProt 1–215 Author chain K; PDBConstruct 2–216; UniProt 1–215

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 2911–3045 Fragment:;RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969) ; Mutation:W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2911–3045 Fragment:;RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969) ; Mutation:W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 2911–3045 Fragment:;RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969) ; Mutation:W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 2911–3045 Fragment:;RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969) ; Mutation:W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 2911–3045 Fragment:;RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969) ; Mutation:W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 2911–3045 Fragment:;RAN-binding domain 4 of the E3 SUMO-PROTEIN LIGASE RANBP2 (UNP residues 2911-3045), WHTMKNYY/QNYDNKQV mutant (UNP residues 2962-2969) ; Mutation:W2962Q, H2963N, T2964Y, M2965D, K2966N, N2967K, Y2928Q, Y2969V 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;pH 7;294 K;20% w/v PEG3350, 0.1 M ammonium sulfate, 0.1 M HEPES Resolution 2.35 Å R-free 0.225

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 5–139; UniProt 2911–3045 Author chain D; PDBConstruct 5–139; UniProt 2911–3045 Author chain F; PDBConstruct 5–139; UniProt 2911–3045 Author chain H; PDBConstruct 5–139; UniProt 2911–3045 Author chain J; PDBConstruct 5–139; UniProt 2911–3045 Author chain L; PDBConstruct 5–139; UniProt 2911–3045

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 7mnz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mnz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7mnz
Deposition date deposition_date2021-05-01
Structure title titleCrystal Structure of Nup358/RanBP2 Ran-binding domain 4 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_electron45.44
Forward intensity I(0) i0826401000.00
Molecular weight molecular_weight239070.0 kDa
Excluded volume excluded_volume300060 ų
Envelope volume envelope_volume417380 ų
Hydration-shell volume shell_volume76982 ų
Envelope diameter envelope_diameter167.9
Shell Rg shell_rg49.51
Envelope Rg envelope_rg44.88
Shape Rg shape_rg45.43
Total Rg total_rg45.64
Total atoms total_atoms33569
Residues n_residues2060
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 dmax156.6
Rg (real space) rg_real45.60
Rg uncertainty (real space) rg_real_error1.88
I(0) (real space) i0_real8.2640e+08
I(0) uncertainty (real space) i0_real_error1.6090e+07
Rg (reciprocal space) rg_reciprocal45.67
I(0) (reciprocal space) i0_reciprocal826500000.0000
Solution quality estimate total_estimate0.8767
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.7
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57470000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.833; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.898

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)