3gj8

Crystal structure of human RanGDP-Nup153ZnF34 complex

Method: X-RAY DIFFRACTION Dmax: 83.2 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 2–216 Mutation:F35S Nuclear pore complex protein Nup153 × 1 (P49791) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.1M Bis-Tris pH 6.5, 18-20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.82 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2–216 Mutation:F35S Nuclear pore complex protein Nup153 × 1 (P49791) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.1M Bis-Tris pH 6.5, 18-20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.82 Å R-free 0.203

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 7–221; UniProt 2–216 Author chain C; PDBConstruct 7–221; UniProt 2–216

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 790–876 Fragment:Nup153 - Zinc finger module 34: UNP residues 790-876 GTP-binding nuclear protein Ran × 1 (P62826) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.1M Bis-Tris pH 6.5, 18-20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.82 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 790–876 Fragment:Nup153 - Zinc finger module 34: UNP residues 790-876 GTP-binding nuclear protein Ran × 1 (P62826) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.1M Bis-Tris pH 6.5, 18-20% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 1.82 Å R-free 0.203

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 6–92; UniProt 790–876 Author chain D; PDBConstruct 6–92; UniProt 790–876

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 3gj8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3gj8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3gj8
Deposition date deposition_date2009-03-07
Structure title titleCrystal structure of human RanGDP-Nup153ZnF34 complex
Keywords keywords;G protein, GDP, Ran, Nup153, Nuclear Pore, Zinc Finger, Acetylation, Cytoplasm, GTP-binding, Host-virus interaction, Isopeptide bond, Nucleotide-binding, Nucleus, Phosphoprotein, Polymorphism, Protein transport, Transport, Ubl conjugation, DNA-binding, Metal-binding, mRNA transport, Nuclear pore complex, Translocation, Zinc, Zinc-finger, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.41
Radius of gyration Rg (electron density) rg_electron25.56
Forward intensity I(0) i046683900.00
Molecular weight molecular_weight52980.0 kDa
Excluded volume excluded_volume66381 ų
Envelope volume envelope_volume80870 ų
Hydration-shell volume shell_volume26750 ų
Envelope diameter envelope_diameter84.3
Shell Rg shell_rg32.62
Envelope Rg envelope_rg25.65
Shape Rg shape_rg25.54
Total Rg total_rg26.44
Total atoms total_atoms3714
Residues n_residues461
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 dmax83.2
Rg (real space) rg_real26.40
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real4.6680e+07
I(0) uncertainty (real space) i0_real_error6.8070e+05
Rg (reciprocal space) rg_reciprocal26.41
I(0) (reciprocal space) i0_reciprocal46680000.0000
Solution quality estimate total_estimate0.7420
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.600
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5418000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.983; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3gj8a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3gj8b_
Class classg — Small proteins
Fold Fold foldg.41 — Rubredoxin-like
Superfamily Superfamily superfamilyg.41.11 — Ran binding protein zinc finger-like
Family Family familyg.41.11.1 — Ran binding protein zinc finger-like
Domain ID domain_idd3gj8c_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd3gj8d_
Class classg — Small proteins
Fold Fold foldg.41 — Rubredoxin-like
Superfamily Superfamily superfamilyg.41.11 — Ran binding protein zinc finger-like
Family Family familyg.41.11.1 — Ran binding protein zinc finger-like

CATH v4.4 (2 domains)

Domain ID domain_id3gj8A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3gj8C00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)