8adl

Cryo-EM structure of the SEA complex

Method: ELECTRON MICROSCOPY Dmax: 252.3 Å Quality: EXCELLENT

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

Maintenance of telomere capping protein 5

OrganismNot specified

UniProt Q03897

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain C; UniProt 1–1148 Chain Q; UniProt 1–1148 Not recorded Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 WDR59_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–1148; UniProt 1–1148 Author chain Q; PDBConstruct 1–1148; UniProt 1–1148

Nucleoporin SEH1

OrganismNot specified

UniProt P53011

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain D; UniProt 1–349 Chain E; UniProt 1–349 Chain F; UniProt 1–349 Chain L; UniProt 1–349 Chain M; UniProt 1–349 Chain N; UniProt 1–349 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) SEH-associated protein 4 × 4 (P38164) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEH1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–349; UniProt 1–349 Author chain E; PDBConstruct 1–349; UniProt 1–349 Author chain F; PDBConstruct 1–349; UniProt 1–349 Author chain L; PDBConstruct 1–349; UniProt 1–349 Author chain M; PDBConstruct 1–349; UniProt 1–349 Author chain N; PDBConstruct 1–349; UniProt 1–349

SEH-associated protein 4

OrganismNot specified

UniProt P38164

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain B; UniProt 1–1038 Chain G; UniProt 1–1038 Chain J; UniProt 1–1038 Chain O; UniProt 1–1038 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Nucleoporin SEH1 × 6 (P53011) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEA4_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–1038; UniProt 1–1038 Author chain G; PDBConstruct 1–1038; UniProt 1–1038 Author chain J; PDBConstruct 1–1038; UniProt 1–1038 Author chain O; PDBConstruct 1–1038; UniProt 1–1038

Protein transport protein SEC13

OrganismNot specified

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain H; UniProt 1–297 Chain P; UniProt 1–297 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) Restriction of telomere capping protein 1 × 2 (Q08281) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 4
Chains and sequence ranges Author chain H; PDBConstruct 1–297; UniProt 1–297 Author chain P; PDBConstruct 1–297; UniProt 1–297

Restriction of telomere capping protein 1

OrganismNot specified

UniProt Q08281

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain A; UniProt 1–1341 Chain I; UniProt 1–1341 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) Protein transport protein SEC13 × 2 (Q04491) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RTC1_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain A; PDBConstruct 1–1341; UniProt 1–1341 Author chain I; PDBConstruct 1–1341; UniProt 1–1341

Nitrogen permease regulator 3

OrganismNot specified

UniProt P38742

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain U; UniProt 1–1146 Chain V; UniProt 1–1146 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Vacuolar membrane-associated protein IML1 × 2 (P47170) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 NPR3_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain U; PDBConstruct 1–1146; UniProt 1–1146 Author chain V; PDBConstruct 1–1146; UniProt 1–1146

Vacuolar membrane-associated protein IML1

OrganismNot specified

UniProt P47170

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain W; UniProt 1–1584 Chain X; UniProt 1–1584 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nitrogen permease regulator 3 × 2 (P38742) Nitrogen permease regulator 2 × 2 (P39923) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 IML1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain W; PDBConstruct 1–1584; UniProt 1–1584 Author chain X; PDBConstruct 1–1584; UniProt 1–1584

Nitrogen permease regulator 2

OrganismNot specified

UniProt P39923

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain S; UniProt 1–615 Chain T; UniProt 1–615 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) ZN ZINC ION × 28 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 NPR2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain S; PDBConstruct 1–615; UniProt 1–615 Author chain T; PDBConstruct 1–615; UniProt 1–615

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 8adl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8adl
Deposition date deposition_date2022-07-08
Structure title titleCryo-EM structure of the SEA complex
Keywords keywordsGTPase activating protein, coatomer, TOR signaling, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron104.00
Forward intensity I(0) i026511500000.00
Molecular weight molecular_weight1406500.0 kDa
Excluded volume excluded_volume1764700 ų
Envelope volume envelope_volume3315500 ų
Hydration-shell volume shell_volume272350 ų
Envelope diameter envelope_diameter316.8
Shell Rg shell_rg96.42
Envelope Rg envelope_rg97.64
Shape Rg shape_rg104.00
Total Rg total_rg103.90
Total atoms total_atoms98972
Residues n_residues12238
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 dmax252.3
Rg (real space) rg_real100.90
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real2.5530e+10
I(0) uncertainty (real space) i0_real_error5.0010e+08
Rg (reciprocal space) rg_reciprocal105.70
I(0) (reciprocal space) i0_reciprocal26630000000.0000
Solution quality estimate total_estimate0.9148
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary117.7
Skewness Skewness skewness-0.005
Kurtosis Kurtosis kurtosis-0.706
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha0.3734
Highest regularization parameter α highest_alpha564500000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.966; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8adlB01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8adlG01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8adlJ01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id8adlO01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)