3fmo

Crystal structure of the nucleoporin Nup214 in complex with the DEAD-box helicase Ddx19

Method: X-RAY DIFFRACTION Dmax: 92.8 Å Quality: GOOD

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

Nuclear pore complex protein Nup214

Homo sapiens

UniProt P35658

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 1–450 Not recorded ATP-dependent RNA helicase DDX19B × 1 (Q9UMR2) GOL GLYCEROL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;298 K;sodium di-hydrogen phosphate, di-potassium hydrogen phosphate, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.51 Å R-free 0.242

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 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU214_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–450; UniProt 1–450

ATP-dependent RNA helicase DDX19B

Homo sapiens

UniProt Q9UMR2

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 1–300 Not recorded Nuclear pore complex protein Nup214 × 1 (P35658) GOL GLYCEROL × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;298 K;sodium di-hydrogen phosphate, di-potassium hydrogen phosphate, sodium acetate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.51 Å R-free 0.242

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DD19B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–300; UniProt 1–300

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 3fmo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3fmo
Deposition date deposition_date2008-12-22
Structure title titleCrystal structure of the nucleoporin Nup214 in complex with the DEAD-box helicase Ddx19
Keywords keywords;nuclear porin, nuclear pore complex, nucleocytoplasmic transport, mRNA export, protein interaction, helicase, beta-propeller, DEAD box, Glycoprotein, mRNA transport, Nucleus, Phosphoprotein, Protein transport, Proto-oncogene, Translocation, Transport, ATP-binding, Hydrolase, Membrane, Nucleotide-binding, RNA-binding, Protein transport-Hydrolase COMPLEX, Oncoprotein-Hydrolase COMPLEX ;; Oncoprotein/Hydrolase
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.89
Radius of gyration Rg (electron density) rg_electron28.27
Forward intensity I(0) i082868100.00
Molecular weight molecular_weight73412.0 kDa
Excluded volume excluded_volume92779 ų
Envelope volume envelope_volume114600 ų
Hydration-shell volume shell_volume34392 ų
Envelope diameter envelope_diameter97.5
Shell Rg shell_rg35.11
Envelope Rg envelope_rg28.40
Shape Rg shape_rg28.27
Total Rg total_rg28.95
Total atoms total_atoms5151
Residues n_residues653
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 dmax92.8
Rg (real space) rg_real28.96
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real8.2870e+07
I(0) uncertainty (real space) i0_real_error1.2150e+06
Rg (reciprocal space) rg_reciprocal28.93
I(0) (reciprocal space) i0_reciprocal82870000.0000
Solution quality estimate total_estimate0.8786
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.4
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29220000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.828

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_idd3fmob_
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 (1 domains)

Domain ID domain_id3fmoB00
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)