6qg5

Structure of eIF2B-eIF2 (phosphorylated at Ser51) complex (model C)

Method: ELECTRON MICROSCOPY Dmax: 215.3 Å Quality: GOOD

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

Translation initiation factor eIF-2B subunit alpha

Saccharomyces cerevisiae

UniProt P14741

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–305 Chain B; UniProt 1–305 Not recorded Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BA_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–305; UniProt 1–305 Author chain B; PDBConstruct 1–305; UniProt 1–305

Translation initiation factor eIF-2B subunit beta

Saccharomyces cerevisiae

UniProt P32502

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain C; UniProt 1–381 Chain D; UniProt 1–381 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BB_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–381; UniProt 1–381 Author chain D; PDBConstruct 1–381; UniProt 1–381

Translation initiation factor eIF-2B subunit gamma

Saccharomyces cerevisiae

UniProt P09032

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain E; UniProt 1–578 Chain F; UniProt 1–578 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BG_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–578; UniProt 1–578 Author chain F; PDBConstruct 1–578; UniProt 1–578

Translation initiation factor eIF-2B subunit delta

Saccharomyces cerevisiae

UniProt P12754

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain G; UniProt 1–651 Chain H; UniProt 1–651 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BD_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–651; UniProt 1–651 Author chain H; PDBConstruct 1–651; UniProt 1–651

Translation initiation factor eIF-2B subunit epsilon

Saccharomyces cerevisiae

UniProt P32501

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain I; UniProt 1–712 Chain J; UniProt 1–712 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

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

View Construct and Data Evidence
UniProt name EI2BE_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–712; UniProt 1–712 Author chain J; PDBConstruct 1–712; UniProt 1–712

Eukaryotic translation initiation factor 2 subunit alpha

Saccharomyces cerevisiae

UniProt P20459

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain K; UniProt 1–304 Chain L; UniProt 1–304 Non-standard monomer:Yes (specific site not provided by mmCIF) Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2A_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain K; PDBConstruct 1–304; UniProt 1–304 Author chain L; PDBConstruct 1–304; UniProt 1–304

Eukaryotic translation initiation factor 2 subunit gamma

Saccharomyces cerevisiae

UniProt P32481

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain M; UniProt 1–527 Chain N; UniProt 1–527 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit beta × 2 (P09064) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2G_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain M; PDBConstruct 1–527; UniProt 1–527 Author chain N; PDBConstruct 1–527; UniProt 1–527

Eukaryotic translation initiation factor 2 subunit beta

Saccharomyces cerevisiae

UniProt P09064

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain O; UniProt 1–285 Chain P; UniProt 1–285 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (P14741) Translation initiation factor eIF-2B subunit beta × 2 (P32502) Translation initiation factor eIF-2B subunit gamma × 2 (P09032) Translation initiation factor eIF-2B subunit delta × 2 (P12754) Translation initiation factor eIF-2B subunit epsilon × 2 (P32501) Eukaryotic translation initiation factor 2 subunit alpha × 2 (P20459) Eukaryotic translation initiation factor 2 subunit gamma × 2 (P32481) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 10.10 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2B_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain O; PDBConstruct 1–285; UniProt 1–285 Author chain P; PDBConstruct 1–285; UniProt 1–285

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 6qg5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qg5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qg5
Deposition date deposition_date2019-01-10
Structure title titleStructure of eIF2B-eIF2 (phosphorylated at Ser51) complex (model C)
Keywords keywordsintegrated stress response, ISR, translation, initiation factors, phosphorylation, eIF2, eIF2B, tRNAi, GEF, heat domain, eIF2 alpha; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.23
Radius of gyration Rg (electron density) rg_electron71.05
Forward intensity I(0) i03911600000.00
Molecular weight molecular_weight538500.0 kDa
Excluded volume excluded_volume679290 ų
Envelope volume envelope_volume1158800 ų
Hydration-shell volume shell_volume140940 ų
Envelope diameter envelope_diameter273.7
Shell Rg shell_rg65.09
Envelope Rg envelope_rg72.75
Shape Rg shape_rg70.99
Total Rg total_rg71.14
Total atoms total_atoms37875
Residues n_residues4851
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 dmax215.3
Rg (real space) rg_real68.28
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real3.8560e+09
I(0) uncertainty (real space) i0_real_error7.1910e+07
Rg (reciprocal space) rg_reciprocal68.49
I(0) (reciprocal space) i0_reciprocal3895000000.0000
Solution quality estimate total_estimate0.8402
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.5
Skewness Skewness skewness0.525
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0873
Highest regularization parameter α highest_alpha364400000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.132

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)