2c1m

Nup50:importin-alpha complex

Method: X-RAY DIFFRACTION Dmax: 101.9 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

IMPORTIN-ALPHA2 SUBUNIT

MUS MUSCULUS

UniProt P52293

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 75–498 Fragment:DELTA IBB, RESIDUES 75-498 NUCLEOPORIN 50 KDA × 1 (Q9JIH2) X-RAY DIFFRACTION X-ray crystallization conditions:DETAILS GIVEN IN PUBLICATION Resolution 2.20 Å R-free 0.254

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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMA2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–424; UniProt 75–498

NUCLEOPORIN 50 KDA

MUS MUSCULUS

UniProt Q9JIH2

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 1–46 Fragment:RESIDUES 1-46 IMPORTIN-ALPHA2 SUBUNIT × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:DETAILS GIVEN IN PUBLICATION Resolution 2.20 Å R-free 0.254

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name NUP50_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–46; UniProt 1–46

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 2c1m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2c1m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2c1m
Deposition date deposition_date2005-09-16
Structure title titleNup50:importin-alpha complex
Keywords keywords;PROTEIN TRANSPORT/MEMBRANE PROTEIN, NUCLEAR TRANSPORT-COMPLEX, IMPORTIN-ALPHA, NUCLEOPORIN NUP50, NUCLEAR TRANSPORT-COMPLEX NUP50, NUCLEAR PROTEIN, PROTEIN TRANSPORT, PROTEIN TRANSPORT-MEMBRANE PROTEIN complex ;; PROTEIN TRANSPORT/MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.57
Radius of gyration Rg (electron density) rg_electron29.52
Forward intensity I(0) i041459300.00
Molecular weight molecular_weight51361.0 kDa
Excluded volume excluded_volume64797 ų
Envelope volume envelope_volume79926 ų
Hydration-shell volume shell_volume24960 ų
Envelope diameter envelope_diameter108.4
Shell Rg shell_rg33.36
Envelope Rg envelope_rg29.80
Shape Rg shape_rg29.50
Total Rg total_rg29.94
Total atoms total_atoms3612
Residues n_residues470
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 dmax101.9
Rg (real space) rg_real29.94
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real4.1460e+07
I(0) uncertainty (real space) i0_real_error5.9510e+05
Rg (reciprocal space) rg_reciprocal29.79
I(0) (reciprocal space) i0_reciprocal41450000.0000
Solution quality estimate total_estimate0.7852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.604
Kurtosis Kurtosis kurtosis-0.289
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11860000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.656; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.616; Smooth: 0.618

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2c1ma_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.1 — Armadillo repeat

CATH v4.4 (1 domains)

Domain ID domain_id2c1mA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)