9zmy

Crystal structure of the human Commd10 HN domain in domain swapped conformation

Method: X-RAY DIFFRACTION Dmax: 118.7 Å Quality: REASONABLE

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

COMM domain-containing protein 10

Homo sapiens

UniProt Q9Y6G5

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 12–127 Chain B; UniProt 12–127 Fragment:HN domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 8;293 K;30% PEG400 in 0.1 M Tris pH 8.0 Resolution 1.62 Å R-free 0.241

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 COMDA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–116; UniProt 12–127 Author chain B; PDBConstruct 1–116; UniProt 12–127

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 9zmy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9zmy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9zmy
Deposition date deposition_date2025-12-11
最后修订 last_revision2026-01-21
Structure title titleCrystal structure of the human Commd10 HN domain in domain swapped conformation
Keywords keywordsCOMMD, Commander, endosome, EXOCYTOSIS; EXOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.91
Radius of gyration Rg (electron density) rg_electron32.00
Forward intensity I(0) i011415500.00
Molecular weight molecular_weight25991.0 kDa
Excluded volume excluded_volume32773 ų
Envelope volume envelope_volume54710 ų
Hydration-shell volume shell_volume17048 ų
Envelope diameter envelope_diameter121.5
Shell Rg shell_rg31.55
Envelope Rg envelope_rg32.91
Shape Rg shape_rg31.89
Total Rg total_rg32.31
Total atoms total_atoms1833
Residues n_residues227
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 dmax118.7
Rg (real space) rg_real31.68
Rg uncertainty (real space) rg_real_error1.66
I(0) (real space) i0_real1.1420e+07
I(0) uncertainty (real space) i0_real_error1.9510e+05
Rg (reciprocal space) rg_reciprocal31.34
I(0) (reciprocal space) i0_reciprocal11410000.0000
Solution quality estimate total_estimate0.7243
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.839
Kurtosis Kurtosis kurtosis0.550
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha699400.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.474; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.279; Smooth: 0.710

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)