3peu

S. cerevisiae Dbp5 L327V C-terminal domain bound to Gle1 H337R and IP6

Method: X-RAY DIFFRACTION Dmax: 78.8 Å Quality: GOOD

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

ATP-dependent RNA helicase DBP5

Saccharomyces cerevisiae

UniProt P20449

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 297–482 Fragment:Dbp5-CTD Mutation:L327V,H337R Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin GLE1 × 1 (Q12315) SO4 SULFATE ION × 1 GOL GLYCEROL × 3 IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;30% PEG 3350, 100 mM HEPES pH 8.0, 50 mM NaOAc, 200mM LiS04, 10 mM HEPES pH 7.5, 100mM NaCl, 1mM DTT, 0.5 mM IP6, 5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.60 Å R-free 0.213
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 297–482 Fragment:Dbp5-CTD Mutation:L327V,H337R Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin GLE1 × 1 (Q12315) SO4 SULFATE ION × 1 GOL GLYCEROL × 3 IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;30% PEG 3350, 100 mM HEPES pH 8.0, 50 mM NaOAc, 200mM LiS04, 10 mM HEPES pH 7.5, 100mM NaCl, 1mM DTT, 0.5 mM IP6, 5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.60 Å R-free 0.213

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DBP5_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–188; UniProt 297–482

Nucleoporin GLE1

Saccharomyces cerevisiae

UniProt Q12315

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 244–538 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP-dependent RNA helicase DBP5 × 1 (P20449) SO4 SULFATE ION × 1 GOL GLYCEROL × 3 IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;30% PEG 3350, 100 mM HEPES pH 8.0, 50 mM NaOAc, 200mM LiS04, 10 mM HEPES pH 7.5, 100mM NaCl, 1mM DTT, 0.5 mM IP6, 5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.60 Å R-free 0.213
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 244–538 Non-standard monomer:Yes (specific site not provided by mmCIF) ATP-dependent RNA helicase DBP5 × 1 (P20449) SO4 SULFATE ION × 1 GOL GLYCEROL × 3 IHP INOSITOL HEXAKISPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;30% PEG 3350, 100 mM HEPES pH 8.0, 50 mM NaOAc, 200mM LiS04, 10 mM HEPES pH 7.5, 100mM NaCl, 1mM DTT, 0.5 mM IP6, 5% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.60 Å R-free 0.213

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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLE1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–297; UniProt 244–538

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 3peu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3peu
Deposition date deposition_date2010-10-27
Structure title titleS. cerevisiae Dbp5 L327V C-terminal domain bound to Gle1 H337R and IP6
Keywords keywordsRecA, HEAT, DEAD-box, ATPase, Helicase, mRNA export, Nuclear Pore, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.42
Radius of gyration Rg (electron density) rg_electron23.37
Forward intensity I(0) i051761300.00
Molecular weight molecular_weight55605.0 kDa
Excluded volume excluded_volume69439 ų
Envelope volume envelope_volume82063 ų
Hydration-shell volume shell_volume28858 ų
Envelope diameter envelope_diameter80.5
Shell Rg shell_rg31.00
Envelope Rg envelope_rg23.51
Shape Rg shape_rg23.40
Total Rg total_rg24.15
Total atoms total_atoms3867
Residues n_residues462
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 dmax78.8
Rg (real space) rg_real24.30
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real5.1760e+07
I(0) uncertainty (real space) i0_real_error6.2810e+05
Rg (reciprocal space) rg_reciprocal24.33
I(0) (reciprocal space) i0_reciprocal51760000.0000
Solution quality estimate total_estimate0.8956
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16210000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3peua_
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.37.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id3peuA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3peuB00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily510 — GLE1-like

8. Citations (1)

9. Files and Curves (10)