6zg6

COPII on membranes, outer coat vertex

Method: ELECTRON MICROSCOPY Dmax: 171.2 Å Quality: GOOD

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

Protein transport protein SEC31

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P38968

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–1273 Chain C; UniProt 1–1273 Chain E; UniProt 1–1273 Chain G; UniProt 1–1273 Not recorded Protein transport protein SEC13 × 4 (Q04491) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 12.00 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC31_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1273; UniProt 1–1273 Author chain C; PDBConstruct 1–1273; UniProt 1–1273 Author chain E; PDBConstruct 1–1273; UniProt 1–1273 Author chain G; PDBConstruct 1–1273; UniProt 1–1273

Protein transport protein SEC13

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q04491

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–297 Chain D; UniProt 1–297 Chain F; UniProt 1–297 Chain H; UniProt 1–297 Not recorded Protein transport protein SEC31 × 4 (P38968) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 12.00 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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–297; UniProt 1–297 Author chain D; PDBConstruct 1–297; UniProt 1–297 Author chain F; PDBConstruct 1–297; UniProt 1–297 Author chain H; 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 6zg6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6zg6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6zg6
Deposition date deposition_date2020-06-18
Structure title titleCOPII on membranes, outer coat vertex
Keywords keywordsPROTEIN TRANSPORT, SECRETION, TRAFFICKING; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.07
Radius of gyration Rg (electron density) rg_electron53.57
Forward intensity I(0) i01229280000.00
Molecular weight molecular_weight291450.0 kDa
Excluded volume excluded_volume363560 ų
Envelope volume envelope_volume509810 ų
Hydration-shell volume shell_volume79072 ų
Envelope diameter envelope_diameter180.6
Shell Rg shell_rg55.79
Envelope Rg envelope_rg53.27
Shape Rg shape_rg53.58
Total Rg total_rg53.59
Total atoms total_atoms20612
Residues n_residues2648
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 dmax171.2
Rg (real space) rg_real53.03
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real1.2290e+09
I(0) uncertainty (real space) i0_real_error2.1860e+07
Rg (reciprocal space) rg_reciprocal53.09
I(0) (reciprocal space) i0_reciprocal1229000000.0000
Solution quality estimate total_estimate0.8572
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.2
Skewness Skewness skewness0.200
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63460000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.428

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)