1xip

Crystal Structure of the N-terminal Domain of Nup159

Method: X-RAY DIFFRACTION Dmax: 64.7 Å Quality: EXCELLENT

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

Nucleoporin NUP159

Saccharomyces cerevisiae

UniProt P40477

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–387 Fragment:N-terminal domain Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;292 K;PEG3350, ammonium acetate, sodium acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 2.50 Å R-free 0.249

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.

5 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU159_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–388; UniProt 2–387

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 1xip

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xip
Deposition date deposition_date2004-09-21
Structure title titleCrystal Structure of the N-terminal Domain of Nup159
Keywords keywordsbeta-propeller, 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_guinier21.39
Radius of gyration Rg (electron density) rg_electron19.96
Forward intensity I(0) i027508700.00
Molecular weight molecular_weight40964.0 kDa
Excluded volume excluded_volume51507 ų
Envelope volume envelope_volume60813 ų
Hydration-shell volume shell_volume24418 ų
Envelope diameter envelope_diameter66.9
Shell Rg shell_rg27.43
Envelope Rg envelope_rg20.21
Shape Rg shape_rg19.97
Total Rg total_rg20.90
Total atoms total_atoms2883
Residues n_residues364
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 dmax64.7
Rg (real space) rg_real21.21
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real2.7510e+07
I(0) uncertainty (real space) i0_real_error2.9600e+05
Rg (reciprocal space) rg_reciprocal21.25
I(0) (reciprocal space) i0_reciprocal27510000.0000
Solution quality estimate total_estimate0.9039
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.084
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8131000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1xipa1
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.14 — Nucleoporin domain
Family Family familyb.69.14.1 — Nucleoporin domain
Domain ID domain_idd1xipa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1xipA00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)