5jiu

The crystal structure of RanBPM/9 IUS-SPRY domain in complex with DDX-4 peptide

Method: X-RAY DIFFRACTION Dmax: 87.8 Å Quality: GOOD

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

Ran-binding protein 9

Homo sapiens

UniProt Q96S59

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 108–350 Chain B; UniProt 108–350 Fragment:UNP RESIDUES 108-350 Probable ATP-dependent RNA helicase DDX4 × 2 (Q61496) CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;20~25% (w/v) PEG 3350, 0.1 M Bis-Tris, pH 6.5, 0.2 M NaCl Resolution 2.05 Å R-free 0.203

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RANB9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–243; UniProt 108–350 Author chain B; PDBConstruct 1–243; UniProt 108–350

Probable ATP-dependent RNA helicase DDX4

OrganismNot specified

UniProt Q61496

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 201–220 Chain D; UniProt 201–220 Fragment:UNP RESIDUES 201-220 Ran-binding protein 9 × 2 (Q96S59) CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;20~25% (w/v) PEG 3350, 0.1 M Bis-Tris, pH 6.5, 0.2 M NaCl Resolution 2.05 Å R-free 0.203

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name DDX4_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–20; UniProt 201–220 Author chain D; PDBConstruct 1–20; UniProt 201–220

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 5jiu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5jiu
Deposition date deposition_date2016-04-22
Structure title titleThe crystal structure of RanBPM/9 IUS-SPRY domain in complex with DDX-4 peptide
Keywords keywordsbeta sandwich, Ran binding protein, TRANSPORT PROTEIN, RAN BINDING PROTEIN-PEPTIDE complex; RAN BINDING PROTEIN/PEPTIDE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.81
Radius of gyration Rg (electron density) rg_electron26.27
Forward intensity I(0) i040430400.00
Molecular weight molecular_weight48003.0 kDa
Excluded volume excluded_volume59373 ų
Envelope volume envelope_volume69733 ų
Hydration-shell volume shell_volume23510 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg31.76
Envelope Rg envelope_rg26.16
Shape Rg shape_rg26.29
Total Rg total_rg26.81
Total atoms total_atoms3384
Residues n_residues430
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 dmax87.8
Rg (real space) rg_real27.04
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real4.0430e+07
I(0) uncertainty (real space) i0_real_error5.8180e+05
Rg (reciprocal space) rg_reciprocal26.97
I(0) (reciprocal space) i0_reciprocal40430000.0000
Solution quality estimate total_estimate0.8316
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.474
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13830000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.712; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5jiuA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily920 — SPRY domain
Domain ID domain_id5jiuB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily920 — SPRY domain

8. Citations (1)

9. Files and Curves (10)