3fhc

Crystal structure of human Dbp5 in complex with Nup214

Method: X-RAY DIFFRACTION Dmax: 93.5 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 1–405 Fragment:Nterminal beta propeller, UNP residues 1-405 ATP-dependent RNA helicase DDX19B × 1 (Q9UMR2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;50mM MES pH 6.0, 900mM Na citrate, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.80 Å R-free 0.260

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 1–405; UniProt 1–405

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 68–302 Fragment:Nterminal RecA-like domain, UNP residues 68-302 Nuclear pore complex protein Nup214 × 1 (P35658) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;50mM MES pH 6.0, 900mM Na citrate, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.80 Å R-free 0.260

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 1–235; UniProt 68–302

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 3fhc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3fhc
Deposition date deposition_date2008-12-09
Structure title titleCrystal structure of human Dbp5 in complex with Nup214
Keywords keywords;DEAD-box helicase, mRNA export, Nucleoporin, beta propeller, RecA-like, RNA dependent ATPase, CAN, Ddx19, Dead-box protein 19b, nuclear pore complex, Glycoprotein, mRNA transport, Nucleus, Phosphoprotein, Protein transport, Proto-oncogene, Translocation, Transport, ATP-binding, Helicase, Hydrolase, Membrane, Nucleotide-binding, RNA-binding, TRANSPORT PROTEIN-HYDROLASE COMPLEX ;; TRANSPORT PROTEIN/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.03
Radius of gyration Rg (electron density) rg_electron27.62
Forward intensity I(0) i068804600.00
Molecular weight molecular_weight67437.0 kDa
Excluded volume excluded_volume85519 ų
Envelope volume envelope_volume105120 ų
Hydration-shell volume shell_volume32380 ų
Envelope diameter envelope_diameter96.8
Shell Rg shell_rg34.49
Envelope Rg envelope_rg27.85
Shape Rg shape_rg27.62
Total Rg total_rg28.34
Total atoms total_atoms4736
Residues n_residues605
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 dmax93.5
Rg (real space) rg_real28.15
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real6.8800e+07
I(0) uncertainty (real space) i0_real_error1.0520e+06
Rg (reciprocal space) rg_reciprocal28.12
I(0) (reciprocal space) i0_reciprocal68800000.0000
Solution quality estimate total_estimate0.8687
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.5
Skewness Skewness skewness0.484
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29930000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.914

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3fhcb_
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_id3fhcB00
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)