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6xe6

Structure of Human Dispatched-1 (DISP1)

Method: ELECTRON MICROSCOPY Dmax: 116.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Protein dispatched homolog 1

Homo sapiens

UniProt Q96F81

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 A； UniProt 172–1249 Not recorded Y01 CHOLESTEROL HEMISUCCINATE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 4.53 Å

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.

Other PDB Difference from Current Entry 6XE6 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7E2G Cryo-EM structure of hDisp1NNN-3C Deposited 2021-02-05 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 1–262（262 aa）
Chain D 281–1524（1244 aa）
Mutation：D572N,D573N,D1051N Mutation：D572N,D573N,D1051N Y01 CHOLESTEROL HEMISUCCINATE × 11 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.61 Å
7E2H Cryo-EM structure of hDisp1NNN-3C-Cleavage Deposited 2021-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain D 1–262（262 aa）
Chain E 281–1524（1244 aa）
Mutation：D572N,D573N,D1051N Y01 CHOLESTEROL HEMISUCCINATE × 8 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.68 Å
7E2I Cryo-EM structure of hDisp1NNN-ShhN Deposited 2021-02-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–1524（1524 aa）
Mutation：D572N,D573N,D1051N ZN ZINC ION × 1 Y01 CHOLESTEROL HEMISUCCINATE × 7 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.07 Å

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

View Construct and Data Evidence
UniProt name DISP1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 11–1088； UniProt 172–1249

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 6xe6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xe6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6xe6
Deposition date deposition_date2020-06-12
Structure title titleStructure of Human Dispatched-1 (DISP1)
Keywords keywordshedgehog, secretion, sterol binding, Sterol-sensing domain, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.22 Å
Radius of gyration Rg (electron density) rg_electron34.32 Å
Forward intensity I(0) i0116961000.00
Molecular weight molecular_weight92741.0 kDa
Excluded volume excluded_volume118560 ų
Envelope volume envelope_volume162530 ų
Hydration-shell volume shell_volume40735 ų
Envelope diameter envelope_diameter122.5 Å
Shell Rg shell_rg39.53 Å
Envelope Rg envelope_rg34.70 Å
Shape Rg shape_rg34.31 Å
Total Rg total_rg34.81 Å
Total atoms total_atoms6530
Residues n_residues826
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax116.3 Å
Rg (real space) rg_real35.27 Å
Rg uncertainty (real space) rg_real_error0.91 Å
I(0) (real space) i0_real1.1700e+08
I(0) uncertainty (real space) i0_real_error1.7200e+06
Rg (reciprocal space) rg_reciprocal35.24 Å
I(0) (reciprocal space) i0_reciprocal117000000.0000
Solution quality estimate total_estimate0.8892
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.6 Å
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.521
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30870000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.873
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)