8esd

Crystal structure of COMMD7-COMMD9-COMMD5-COMMD10 tetramer

Method: X-RAY DIFFRACTION Dmax: 100.6 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain T; UniProt 12–202 Not recorded COMM domain-containing protein 9 × 1 (Q9P000) COMM domain-containing protein 5 × 1 (Q9GZQ3) COMM domain-containing protein 7 × 1 (Q86VX2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;2 uM crown ether and 10% glycerol and grown in 22% ethanol and 5 mM EDTA Resolution 3.33 Å R-free 0.278

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 T; PDBConstruct 1–191; UniProt 12–202

COMM domain-containing protein 9

Homo sapiens

UniProt Q9P000

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 N; UniProt 5–198 Not recorded COMM domain-containing protein 10 × 1 (Q9Y6G5) COMM domain-containing protein 5 × 1 (Q9GZQ3) COMM domain-containing protein 7 × 1 (Q86VX2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;2 uM crown ether and 10% glycerol and grown in 22% ethanol and 5 mM EDTA Resolution 3.33 Å R-free 0.278

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.

6 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COMD9_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain N; PDBConstruct 1–194; UniProt 5–198

COMM domain-containing protein 5

Homo sapiens

UniProt Q9GZQ3

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 F; UniProt 149–222 Not recorded COMM domain-containing protein 10 × 1 (Q9Y6G5) COMM domain-containing protein 9 × 1 (Q9P000) COMM domain-containing protein 7 × 1 (Q86VX2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;2 uM crown ether and 10% glycerol and grown in 22% ethanol and 5 mM EDTA Resolution 3.33 Å R-free 0.278

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 COMD5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–74; UniProt 149–222

COMM domain-containing protein 7

Homo sapiens

UniProt Q86VX2

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 S; UniProt 131–200 Not recorded COMM domain-containing protein 10 × 1 (Q9Y6G5) COMM domain-containing protein 9 × 1 (Q9P000) COMM domain-containing protein 5 × 1 (Q9GZQ3) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;2 uM crown ether and 10% glycerol and grown in 22% ethanol and 5 mM EDTA Resolution 3.33 Å R-free 0.278

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 COMD7_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–70; UniProt 131–200

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 8esd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8esd
Deposition date deposition_date2022-10-13
Structure title titleCrystal structure of COMMD7-COMMD9-COMMD5-COMMD10 tetramer
Keywords keywordsComplex, Commander, Retriever, Commd5, Commd7, Commd9, Commd10, Commd, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.67
Radius of gyration Rg (electron density) rg_electron28.96
Forward intensity I(0) i053511400.00
Molecular weight molecular_weight58194.0 kDa
Excluded volume excluded_volume73490 ų
Envelope volume envelope_volume98065 ų
Hydration-shell volume shell_volume29773 ų
Envelope diameter envelope_diameter97.5
Shell Rg shell_rg34.44
Envelope Rg envelope_rg29.36
Shape Rg shape_rg28.93
Total Rg total_rg29.65
Total atoms total_atoms4089
Residues n_residues514
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 dmax100.6
Rg (real space) rg_real29.79
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real5.3510e+07
I(0) uncertainty (real space) i0_real_error9.1090e+05
Rg (reciprocal space) rg_reciprocal29.74
I(0) (reciprocal space) i0_reciprocal53510000.0000
Solution quality estimate total_estimate0.8773
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.2
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.251
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10180000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.836; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.938; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)