9h5k

Cryo-EM structure of the SEAC-EGOC supercomplex

Method: ELECTRON MICROSCOPY Dmax: 347.4 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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain C; UniProt 1–1148 Chain K; UniProt 1–1148 Not recorded Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 K; PDBConstruct 1–1148; UniProt 1–1148

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 × 32 PDB declaration: 32-meric(32) 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) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 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 × 32 PDB declaration: 32-meric(32) 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) Protein transport protein SEC13 × 2 (Q04491) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–1341; UniProt 1–1341 Author chain I; PDBConstruct 1–1341; UniProt 1–1341

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 × 32 PDB declaration: 32-meric(32) 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) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 4
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 × 32 PDB declaration: 32-meric(32) 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) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 5
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

GTP-binding protein GTR1

Saccharomyces cerevisiae

UniProt Q00582

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain a; UniProt 1–310 Chain b; UniProt 1–310 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name RAGAB_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain a; PDBConstruct 1–310; UniProt 1–310 Author chain b; PDBConstruct 1–310; UniProt 1–310

GTP-binding protein GTR2

Saccharomyces cerevisiae

UniProt P53290

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain c; UniProt 1–341 Chain d; UniProt 1–341 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name RAGCD_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain c; PDBConstruct 1–341; UniProt 1–341 Author chain d; PDBConstruct 1–341; UniProt 1–341

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain T; UniProt 1–615 Chain g; UniProt 1–615 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 T; PDBConstruct 1–615; UniProt 1–615 Author chain g; PDBConstruct 1–615; UniProt 1–615

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain h; UniProt 1–1146 Chain i; UniProt 1–1146 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 9
Chains and sequence ranges Author chain h; PDBConstruct 1–1146; UniProt 1–1146 Author chain i; 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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain X; UniProt 1–1584 Chain j; UniProt 1–1584 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 10
Chains and sequence ranges Author chain X; PDBConstruct 1–1584; UniProt 1–1584 Author chain j; PDBConstruct 1–1584; UniProt 1–1584

Protein MEH1

Saccharomyces cerevisiae

UniProt Q02205

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain R; UniProt 1–184 Chain S; UniProt 1–184 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein EGO2 × 2 (Q3E830) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MEH1_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain R; PDBConstruct 1–184; UniProt 1–184 Author chain S; PDBConstruct 1–184; UniProt 1–184

Protein EGO2

Saccharomyces cerevisiae

UniProt Q3E830

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain U; UniProt 1–75 Chain W; UniProt 1–75 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein SLM4 × 2 (P38247) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EGO2_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain U; PDBConstruct 1–75; UniProt 1–75 Author chain W; PDBConstruct 1–75; UniProt 1–75

Protein SLM4

Saccharomyces cerevisiae

UniProt P38247

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 × 32 PDB declaration: 32-meric(32) Consistent with protein copy count Chain Y; UniProt 1–162 Chain Z; UniProt 1–162 Not recorded Maintenance of telomere capping protein 5 × 2 (Q03897) Protein transport protein SEC13 × 2 (Q04491) Restriction of telomere capping protein 1 × 2 (Q08281) Nucleoporin SEH1 × 6 (P53011) SEH-associated protein 4 × 4 (P38164) GTP-binding protein GTR1 × 2 (Q00582) GTP-binding protein GTR2 × 2 (P53290) Nitrogen permease regulator 2 × 2 (P39923) Nitrogen permease regulator 3 × 2 (P38742) Vacuolar membrane-associated protein IML1 × 2 (P47170) Protein MEH1 × 2 (Q02205) Protein EGO2 × 2 (Q3E830) ZN ZINC ION × 28 MG MAGNESIUM ION × 2 AF3 ALUMINUM FLUORIDE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

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

View Construct and Data Evidence
UniProt name SLM4_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain Y; PDBConstruct 1–162; UniProt 1–162 Author chain Z; PDBConstruct 1–162; UniProt 1–162

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 9h5k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9h5k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9h5k
Deposition date deposition_date2024-10-22
Structure title titleCryo-EM structure of the SEAC-EGOC supercomplex
Keywords keywordsCell growth, GTPase activating protein, GTPase, coatomer complex, 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_electron116.10
Forward intensity I(0) i035254800000.00
Molecular weight molecular_weight1625100.0 kDa
Excluded volume excluded_volume2039900 ų
Envelope volume envelope_volume3967700 ų
Hydration-shell volume shell_volume294620 ų
Envelope diameter envelope_diameter392.2
Shell Rg shell_rg99.65
Envelope Rg envelope_rg110.30
Shape Rg shape_rg116.10
Total Rg total_rg116.00
Total atoms total_atoms114318
Residues n_residues14138
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 dmax347.4
Rg (real space) rg_real117.50
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real3.4560e+10
I(0) uncertainty (real space) i0_real_error7.1290e+08
Rg (reciprocal space) rg_reciprocal114.40
I(0) (reciprocal space) i0_reciprocal34980000000.0000
Solution quality estimate total_estimate0.9015
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary133.6
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.627
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha1.9860
Highest regularization parameter α highest_alpha1010000000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.911; 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 (17)

8. Citations (1)

9. Files and Curves (10)