3w3z

Crystal structure of Kap121p bound to RanGTP

Method: X-RAY DIFFRACTION Dmax: 137.2 Å Quality: GOOD

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

Importin subunit beta-3

Saccharomyces cerevisiae

UniProt P32337

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 1–1089 Non-standard monomer:Yes (specific site not provided by mmCIF) GTP-binding nuclear protein Ran × 1 (P62825) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;0.1M MES, 0.2M CaCl2, 10% PEG 20000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.298

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IMB3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1089; UniProt 1–1089

GTP-binding nuclear protein Ran

Canis lupus familiaris

UniProt P62825

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 1–176 Fragment:UNP residues 1-176 Importin subunit beta-3 × 1 (P32337) MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;0.1M MES, 0.2M CaCl2, 10% PEG 20000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.70 Å R-free 0.298

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAN_CANFA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–176; UniProt 1–176

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 3w3z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3w3z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3w3z
Deposition date deposition_date2012-12-28
Structure title titleCrystal structure of Kap121p bound to RanGTP
Keywords keywordsHEAT repeat, nuclear import, PROTEIN TRANSPORT-NUCLEAR PROTEIN complex; PROTEIN TRANSPORT/NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.48
Radius of gyration Rg (electron density) rg_electron40.47
Forward intensity I(0) i0248259000.00
Molecular weight molecular_weight130880.0 kDa
Excluded volume excluded_volume164700 ų
Envelope volume envelope_volume232330 ų
Hydration-shell volume shell_volume49144 ų
Envelope diameter envelope_diameter139.0
Shell Rg shell_rg44.89
Envelope Rg envelope_rg39.05
Shape Rg shape_rg40.50
Total Rg total_rg40.65
Total atoms total_atoms9142
Residues n_residues1162
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 dmax137.2
Rg (real space) rg_real40.55
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real2.4830e+08
I(0) uncertainty (real space) i0_real_error4.6860e+06
Rg (reciprocal space) rg_reciprocal40.48
I(0) (reciprocal space) i0_reciprocal248200000.0000
Solution quality estimate total_estimate0.8815
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.7
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14450000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.918; Smooth: 0.858

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3w3zb_
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

CATH v4.4 (1 domains)

Domain ID domain_id3w3zB00
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)