7mo3

Crystal Structure of the ZnF3 of Nucleoporin NUP153 in complex with Ran-GDP, resolution 2.05 Angstrom

Method: X-RAY DIFFRACTION Dmax: 89.0 Å Quality: REASONABLE

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 Nuclear pore complex protein Nup153 × 1 (P49791) 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 7;294 K;20% w/v PEG3350, 0.1 M Bis-Tris Resolution 2.05 Å R-free 0.228
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–216 Mutation:F35S Nuclear pore complex protein Nup153 × 1 (P49791) 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 7;294 K;20% w/v PEG3350, 0.1 M Bis-Tris Resolution 2.05 Å R-free 0.228

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

Nuclear pore complex protein Nup153

Rattus norvegicus

UniProt P49791

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 781–817 Fragment:ZINC FINGER 3 of NUP153 (UNP residues 781-817) 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 7;294 K;20% w/v PEG3350, 0.1 M Bis-Tris Resolution 2.05 Å R-free 0.228
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 781–817 Fragment:ZINC FINGER 3 of NUP153 (UNP residues 781-817) 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 7;294 K;20% w/v PEG3350, 0.1 M Bis-Tris Resolution 2.05 Å R-free 0.228

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.

12 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU153_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–42; UniProt 781–817 Author chain D; PDBConstruct 6–42; UniProt 781–817

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 7mo3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mo3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mo3
Deposition date deposition_date2021-05-01
Structure title titleCrystal Structure of the ZnF3 of Nucleoporin NUP153 in complex with Ran-GDP, resolution 2.05 Angstrom
Keywords keywordsnuclear pore complex component, nucleocytoplasmic transport, TRANSPORT PROTEIN, complex (small GTPase-nuclear 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_guinier26.57
Radius of gyration Rg (electron density) rg_electron25.66
Forward intensity I(0) i052064000.00
Molecular weight molecular_weight55797.0 kDa
Excluded volume excluded_volume69778 ų
Envelope volume envelope_volume86155 ų
Hydration-shell volume shell_volume28124 ų
Envelope diameter envelope_diameter93.8
Shell Rg shell_rg32.80
Envelope Rg envelope_rg25.91
Shape Rg shape_rg25.65
Total Rg total_rg26.50
Total atoms total_atoms7781
Residues n_residues487
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 dmax89.0
Rg (real space) rg_real26.56
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real5.2060e+07
I(0) uncertainty (real space) i0_real_error7.9640e+05
Rg (reciprocal space) rg_reciprocal26.57
I(0) (reciprocal space) i0_reciprocal52060000.0000
Solution quality estimate total_estimate0.7241
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.319
Kurtosis Kurtosis kurtosis-0.443
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5785000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.972; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)