1y2a

Structure of mammalian importin bound to the non-classical PLSCR1-NLS

Method: X-RAY DIFFRACTION Dmax: 98.4 Å Quality: GOOD

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

Importin alpha-2 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 C; UniProt 70–497 Fragment:residues 70-497 decamer fragment of Phospholipid scramblase 1 × 1 (O15162) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.6-0.7 M sodium citrate, 100 mM Hepes pH 6.0, 10 mM -mercaptoethonal, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.20 Å R-free 0.258

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 C; PDBConstruct 1–428; UniProt 70–497

decamer fragment of Phospholipid scramblase 1

OrganismNot specified

UniProt O15162

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 P; UniProt 257–266 Fragment:NLS Importin alpha-2 Subunit × 1 (P52293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;0.6-0.7 M sodium citrate, 100 mM Hepes pH 6.0, 10 mM -mercaptoethonal, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.20 Å R-free 0.258

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 PLS1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–10; UniProt 257–266

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 1y2a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1y2a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1y2a
Deposition date deposition_date2004-11-22
Structure title titleStructure of mammalian importin bound to the non-classical PLSCR1-NLS
Keywords keywordsArmadillo repeat; protein:peptide complex; superhelix of helices, Protein transport; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.51
Radius of gyration Rg (electron density) rg_electron28.25
Forward intensity I(0) i033956400.00
Molecular weight molecular_weight46963.0 kDa
Excluded volume excluded_volume59478 ų
Envelope volume envelope_volume72898 ų
Hydration-shell volume shell_volume23093 ų
Envelope diameter envelope_diameter101.5
Shell Rg shell_rg33.25
Envelope Rg envelope_rg28.27
Shape Rg shape_rg28.25
Total Rg total_rg28.77
Total atoms total_atoms3307
Residues n_residues433
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 dmax98.4
Rg (real space) rg_real28.88
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real3.3960e+07
I(0) uncertainty (real space) i0_real_error5.2000e+05
Rg (reciprocal space) rg_reciprocal28.77
I(0) (reciprocal space) i0_reciprocal33950000.0000
Solution quality estimate total_estimate0.8018
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.520
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11460000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.682; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.524; Smooth: 0.851

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_idd1y2ac_
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_id1y2aC00
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)