8r2o

Huntingtin-Q17, 1-66, N-MBP fusion

Method: X-RAY DIFFRACTION Dmax: 146.1 Å Quality: REASONABLE

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

Maltodextrin-binding protein,Huntingtin, myristoylated N-terminal fragment

Homo sapiens

UniProt A0A4P1LXE0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–372 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.25;293 K;0.8 M KH2PO4, 0.8 M NaH2PO4, and 0.1 M TRIS/HCl pH 8.25 Resolution 3.23 Å R-free 0.238
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–372 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.25;293 K;0.8 M KH2PO4, 0.8 M NaH2PO4, and 0.1 M TRIS/HCl pH 8.25 Resolution 3.23 Å R-free 0.238

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.

28 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4P1LXE0_SERSF
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–373; UniProt 3–372 Author chain B; PDBConstruct 4–373; UniProt 3–372

Maltodextrin-binding protein,Huntingtin, myristoylated N-terminal fragment

Homo sapiens

UniProt P42858

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–64 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.25;293 K;0.8 M KH2PO4, 0.8 M NaH2PO4, and 0.1 M TRIS/HCl pH 8.25 Resolution 3.23 Å R-free 0.238
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–64 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.25;293 K;0.8 M KH2PO4, 0.8 M NaH2PO4, and 0.1 M TRIS/HCl pH 8.25 Resolution 3.23 Å R-free 0.238

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.

30 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HD_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 383–442; UniProt 1–64 Author chain B; PDBConstruct 383–442; UniProt 1–64

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 8r2o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r2o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r2o
Deposition date deposition_date2023-11-07
Structure title titleHuntingtin-Q17, 1-66, N-MBP fusion
Keywords keywordsHUNTINGTIN, HTT-EX1, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.09
Radius of gyration Rg (electron density) rg_electron45.84
Forward intensity I(0) i0119171000.00
Molecular weight molecular_weight92188.0 kDa
Excluded volume excluded_volume116270 ų
Envelope volume envelope_volume158530 ų
Hydration-shell volume shell_volume30792 ų
Envelope diameter envelope_diameter141.2
Shell Rg shell_rg46.42
Envelope Rg envelope_rg44.34
Shape Rg shape_rg45.83
Total Rg total_rg45.90
Total atoms total_atoms6514
Residues n_residues833
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 dmax146.1
Rg (real space) rg_real45.63
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real1.1920e+08
I(0) uncertainty (real space) i0_real_error2.0300e+06
Rg (reciprocal space) rg_reciprocal45.09
I(0) (reciprocal space) i0_reciprocal119100000.0000
Solution quality estimate total_estimate0.6345
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.309
Kurtosis Kurtosis kurtosis-1.176
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11540000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.136; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.147; Smooth: 0.689

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)