8tqo

Eukaryotic translation initiation factor 2B tetramer

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: GOOD

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

Translation initiation factor eIF-2B subunit epsilon

Homo sapiens

UniProt Q13144

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–721 Not recorded Translation initiation factor eIF-2B subunit gamma × 1 (Q9NR50) Translation initiation factor eIF-2B subunit beta × 1 (P49770) Translation initiation factor eIF-2B subunit delta × 1 (Q9UI10) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–721; UniProt 1–721

Translation initiation factor eIF-2B subunit gamma

Homo sapiens

UniProt Q9NR50

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain I; UniProt 1–452 Not recorded Translation initiation factor eIF-2B subunit epsilon × 1 (Q13144) Translation initiation factor eIF-2B subunit beta × 1 (P49770) Translation initiation factor eIF-2B subunit delta × 1 (Q9UI10) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–452; UniProt 1–452

Translation initiation factor eIF-2B subunit beta

Homo sapiens

UniProt P49770

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 2–351 Not recorded Translation initiation factor eIF-2B subunit epsilon × 1 (Q13144) Translation initiation factor eIF-2B subunit gamma × 1 (Q9NR50) Translation initiation factor eIF-2B subunit delta × 1 (Q9UI10) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name EI2BB_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 19–368; UniProt 2–351

Translation initiation factor eIF-2B subunit delta

Homo sapiens

UniProt Q9UI10

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–523 Not recorded Translation initiation factor eIF-2B subunit epsilon × 1 (Q13144) Translation initiation factor eIF-2B subunit gamma × 1 (Q9NR50) Translation initiation factor eIF-2B subunit beta × 1 (P49770) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name EI2BD_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–523; UniProt 1–523

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 8tqo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tqo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8tqo
Deposition date deposition_date2023-08-08
Structure title titleEukaryotic translation initiation factor 2B tetramer
Keywords keywordsProtein translation, eIF2B, integrated stress response, TRANSLATION; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.17
Radius of gyration Rg (electron density) rg_electron38.65
Forward intensity I(0) i0372325000.00
Molecular weight molecular_weight158360.0 kDa
Excluded volume excluded_volume199130 ų
Envelope volume envelope_volume265080 ų
Hydration-shell volume shell_volume57073 ų
Envelope diameter envelope_diameter134.5
Shell Rg shell_rg44.58
Envelope Rg envelope_rg38.34
Shape Rg shape_rg38.63
Total Rg total_rg39.07
Total atoms total_atoms11122
Residues n_residues1437
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 dmax130.1
Rg (real space) rg_real39.14
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real3.7230e+08
I(0) uncertainty (real space) i0_real_error6.0590e+06
Rg (reciprocal space) rg_reciprocal39.16
I(0) (reciprocal space) i0_reciprocal372300000.0000
Solution quality estimate total_estimate0.8849
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.310
Kurtosis Kurtosis kurtosis-0.363
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha68960000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.879; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.865

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)