8p0x

Structure of the human Commander complex Retriever Subcomplex

Method: ELECTRON MICROSCOPY Dmax: 189.6 Å Quality: GOOD

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

Coiled-coil domain-containing protein 93

OrganismNot specified

UniProt Q567U6

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain K; UniProt 1–631 Not recorded Coiled-coil domain-containing protein 22 × 1 (O60826) Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) VPS35 endosomal protein-sorting factor-like × 1 (Q7Z3J2) Vacuolar protein sorting-associated protein 26C × 1 (O14972) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.50 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.

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

View Construct and Data Evidence
UniProt name CCD93_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain K; PDBConstruct 1–631; UniProt 1–631

Coiled-coil domain-containing protein 22

OrganismNot specified

UniProt O60826

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain L; UniProt 1–627 Not recorded Coiled-coil domain-containing protein 93 × 1 (Q567U6) Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) VPS35 endosomal protein-sorting factor-like × 1 (Q7Z3J2) Vacuolar protein sorting-associated protein 26C × 1 (O14972) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.50 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.

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

View Construct and Data Evidence
UniProt name CCD22_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–627; UniProt 1–627

Vacuolar protein sorting-associated protein 29

OrganismNot specified

UniProt Q9UBQ0

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain N; UniProt 1–182 Not recorded Coiled-coil domain-containing protein 93 × 1 (Q567U6) Coiled-coil domain-containing protein 22 × 1 (O60826) VPS35 endosomal protein-sorting factor-like × 1 (Q7Z3J2) Vacuolar protein sorting-associated protein 26C × 1 (O14972) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.50 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.

20 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS29_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–182; UniProt 1–182

VPS35 endosomal protein-sorting factor-like

OrganismNot specified

UniProt Q7Z3J2

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain O; UniProt 1–963 Not recorded Coiled-coil domain-containing protein 93 × 1 (Q567U6) Coiled-coil domain-containing protein 22 × 1 (O60826) Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) Vacuolar protein sorting-associated protein 26C × 1 (O14972) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.50 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VP35L_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain O; PDBConstruct 1–963; UniProt 1–963

Vacuolar protein sorting-associated protein 26C

OrganismNot specified

UniProt O14972

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain P; UniProt 1–297 Not recorded Coiled-coil domain-containing protein 93 × 1 (Q567U6) Coiled-coil domain-containing protein 22 × 1 (O60826) Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) VPS35 endosomal protein-sorting factor-like × 1 (Q7Z3J2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.50 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.

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

View Construct and Data Evidence
UniProt name VP26C_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain P; PDBConstruct 1–297; UniProt 1–297

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 8p0x

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p0x
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p0x
Deposition date deposition_date2023-05-11
Structure title titleStructure of the human Commander complex Retriever Subcomplex
Keywords keywordsalpha solenoid, arrestin fold, phosphoesterase fold, complex, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.54
Radius of gyration Rg (electron density) rg_electron54.79
Forward intensity I(0) i0355735000.00
Molecular weight molecular_weight130450.0 kDa
Excluded volume excluded_volume151750 ų
Envelope volume envelope_volume351890 ų
Hydration-shell volume shell_volume56688 ų
Envelope diameter envelope_diameter184.6
Shell Rg shell_rg54.70
Envelope Rg envelope_rg51.66
Shape Rg shape_rg54.77
Total Rg total_rg54.82
Total atoms total_atoms9322
Residues n_residues1850
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 dmax189.6
Rg (real space) rg_real54.72
Rg uncertainty (real space) rg_real_error2.61
I(0) (real space) i0_real3.5570e+08
I(0) uncertainty (real space) i0_real_error8.7360e+06
Rg (reciprocal space) rg_reciprocal54.37
I(0) (reciprocal space) i0_reciprocal355500000.0000
Solution quality estimate total_estimate0.8650
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.702
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36180000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.868

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)