7mo0

Crystal Structure of Nucleoporin NUP50 Ran-Binding Domain in Complex with Ran-GPPNHP

Method: X-RAY DIFFRACTION Dmax: 110.8 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 Non-standard monomer:Yes (specific site not provided by mmCIF) Nuclear pore complex protein Nup50 × 1 (Q9UKX7) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;25% w/v PEG3350, 0.2 M ammonium sulfate, 0.1 M HEPES Resolution 2.45 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–216 Non-standard monomer:Yes (specific site not provided by mmCIF) Nuclear pore complex protein Nup50 × 1 (Q9UKX7) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;25% w/v PEG3350, 0.2 M ammonium sulfate, 0.1 M HEPES Resolution 2.45 Å R-free 0.239

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 Nup50

Homo sapiens

UniProt Q9UKX7

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 337–468 Fragment:RAN-binding domain of NUP50 (UNP residues 337-468) Non-standard monomer:Yes (specific site not provided by mmCIF) 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 7.5;294 K;25% w/v PEG3350, 0.2 M ammonium sulfate, 0.1 M HEPES Resolution 2.45 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 337–468 Fragment:RAN-binding domain of NUP50 (UNP residues 337-468) Non-standard monomer:Yes (specific site not provided by mmCIF) GTP-binding nuclear protein Ran × 1 (P62826) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;25% w/v PEG3350, 0.2 M ammonium sulfate, 0.1 M HEPES Resolution 2.45 Å R-free 0.239

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP50_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–134; UniProt 337–468 Author chain D; PDBConstruct 3–134; UniProt 337–468

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 7mo0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mo0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mo0
Deposition date deposition_date2021-05-01
Structure title titleCrystal Structure of Nucleoporin NUP50 Ran-Binding Domain 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_guinier32.69
Radius of gyration Rg (electron density) rg_electron32.35
Forward intensity I(0) i095089700.00
Molecular weight molecular_weight77691.0 kDa
Excluded volume excluded_volume97309 ų
Envelope volume envelope_volume128690 ų
Hydration-shell volume shell_volume34547 ų
Envelope diameter envelope_diameter112.9
Shell Rg shell_rg37.72
Envelope Rg envelope_rg32.11
Shape Rg shape_rg32.33
Total Rg total_rg32.88
Total atoms total_atoms10885
Residues n_residues659
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 dmax110.8
Rg (real space) rg_real32.90
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real9.5090e+07
I(0) uncertainty (real space) i0_real_error1.6940e+06
Rg (reciprocal space) rg_reciprocal32.82
I(0) (reciprocal space) i0_reciprocal95080000.0000
Solution quality estimate total_estimate0.8628
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.444
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34420000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.840; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7mo0B01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id7mo0D01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

8. Citations (1)

9. Files and Curves (10)