6ieg

Crystal structure of human MTR4

Method: X-RAY DIFFRACTION Dmax: 157.4 Å Quality: GOOD

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

Exosome RNA helicase MTR4

Homo sapiens

UniProt P42285

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 71–1042 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;15 mM Tricine pH 8.5, 12% (w/v) PEG 4000 Resolution 3.55 Å R-free 0.305
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 71–1042 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;15 mM Tricine pH 8.5, 12% (w/v) PEG 4000 Resolution 3.55 Å R-free 0.305

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTREX_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 31–1002; UniProt 71–1042 Author chain B; PDBConstruct 31–1002; UniProt 71–1042

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 6ieg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ieg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ieg
Deposition date deposition_date2018-09-14
Structure title titleCrystal structure of human MTR4
Keywords keywordsRNA helicase, MTR4, 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_guinier47.66
Radius of gyration Rg (electron density) rg_electron47.39
Forward intensity I(0) i0498392000.00
Molecular weight molecular_weight184540.0 kDa
Excluded volume excluded_volume230900 ų
Envelope volume envelope_volume366510 ų
Hydration-shell volume shell_volume65228 ų
Envelope diameter envelope_diameter157.3
Shell Rg shell_rg50.81
Envelope Rg envelope_rg45.85
Shape Rg shape_rg47.41
Total Rg total_rg47.47
Total atoms total_atoms12978
Residues n_residues1783
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 dmax157.4
Rg (real space) rg_real47.65
Rg uncertainty (real space) rg_real_error1.99
I(0) (real space) i0_real4.9840e+08
I(0) uncertainty (real space) i0_real_error1.0740e+07
Rg (reciprocal space) rg_reciprocal47.66
I(0) (reciprocal space) i0_reciprocal498400000.0000
Solution quality estimate total_estimate0.8306
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.228
Kurtosis Kurtosis kurtosis-0.613
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28020000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)