5wwo

Crystal structure of Enp1

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: EXCELLENT

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

Essential nuclear protein 1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P38333

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 121–483 Fragment:UNP residues 121-483 Protein LTV1 × 1 (P34078) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;7.2% PEG3350, 12% (v/v) Tacsimate pH 6.0, 8% (v/v) Tacsimate pH 8.0 Resolution 2.40 Å R-free 0.230
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 121–483 Fragment:UNP residues 121-483 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;7.2% PEG3350, 12% (v/v) Tacsimate pH 6.0, 8% (v/v) Tacsimate pH 8.0 Resolution 2.40 Å R-free 0.230

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.

45 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENP1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–363; UniProt 121–483 Author chain B; PDBConstruct 1–363; UniProt 121–483

Protein LTV1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P34078

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 333–463 Fragment:UNP residues 333-463 Essential nuclear protein 1 × 1 (P38333) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;7.2% PEG3350, 12% (v/v) Tacsimate pH 6.0, 8% (v/v) Tacsimate pH 8.0 Resolution 2.40 Å R-free 0.230

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LTV1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–131; UniProt 333–463

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 5wwo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wwo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wwo
Deposition date deposition_date2017-01-03
Structure title titleCrystal structure of Enp1
Keywords keywordscomponent of 90S preribosome, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.06
Radius of gyration Rg (electron density) rg_electron26.75
Forward intensity I(0) i062393000.00
Molecular weight molecular_weight64982.0 kDa
Excluded volume excluded_volume82705 ų
Envelope volume envelope_volume100370 ų
Hydration-shell volume shell_volume31465 ų
Envelope diameter envelope_diameter90.1
Shell Rg shell_rg33.93
Envelope Rg envelope_rg26.94
Shape Rg shape_rg26.72
Total Rg total_rg27.64
Total atoms total_atoms4603
Residues n_residues561
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 dmax84.2
Rg (real space) rg_real27.92
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real6.2390e+07
I(0) uncertainty (real space) i0_real_error8.2420e+05
Rg (reciprocal space) rg_reciprocal27.97
I(0) (reciprocal space) i0_reciprocal62400000.0000
Solution quality estimate total_estimate0.9142
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.9
Skewness Skewness skewness0.133
Kurtosis Kurtosis kurtosis-0.608
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11960000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.981; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)