6ezo

Eukaryotic initiation factor EIF2B in complex with ISRIB

Method: ELECTRON MICROSCOPY Dmax: 170.2 Å Quality: GOOD

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

Translation initiation factor eIF-2B subunit alpha

OrganismNot specified

UniProt Q14232

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 × 10 PDB declaration: decameric(10) 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 (P49770) Translation initiation factor eIF-2B subunit gamma × 2 (Q9NR50) Translation initiation factor eIF-2B subunit delta × 2 (Q9UI10) Human eukaryotic initiation factor EIF2B epsilon subunits × 2 (Q13144) C7B 2-(4-chloranylphenoxy)-~{N}-[4-[2-(4-chloranylphenoxy)ethanoylamino]cyclohexyl]ethanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EI2BA_HUMAN
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

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 5–351 Chain D; UniProt 5–351 Mutation:3xFLAG inserted at position +4 of the protein sequence Translation initiation factor eIF-2B subunit alpha × 2 (Q14232) Translation initiation factor eIF-2B subunit gamma × 2 (Q9NR50) Translation initiation factor eIF-2B subunit delta × 2 (Q9UI10) Human eukaryotic initiation factor EIF2B epsilon subunits × 2 (Q13144) C7B 2-(4-chloranylphenoxy)-~{N}-[4-[2-(4-chloranylphenoxy)ethanoylamino]cyclohexyl]ethanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 2
Chains and sequence ranges Author chain C; PDBConstruct 27–373; UniProt 5–351 Author chain D; PDBConstruct 27–373; UniProt 5–351

Translation initiation factor eIF-2B subunit gamma

OrganismNot specified

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 1–452 Chain F; UniProt 1–452 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (Q14232) Translation initiation factor eIF-2B subunit beta × 2 (P49770) Translation initiation factor eIF-2B subunit delta × 2 (Q9UI10) Human eukaryotic initiation factor EIF2B epsilon subunits × 2 (Q13144) C7B 2-(4-chloranylphenoxy)-~{N}-[4-[2-(4-chloranylphenoxy)ethanoylamino]cyclohexyl]ethanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 3
Chains and sequence ranges Author chain E; PDBConstruct 1–452; UniProt 1–452 Author chain F; PDBConstruct 1–452; UniProt 1–452

Translation initiation factor eIF-2B subunit delta

OrganismNot specified

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–523 Chain H; UniProt 1–523 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (Q14232) Translation initiation factor eIF-2B subunit beta × 2 (P49770) Translation initiation factor eIF-2B subunit gamma × 2 (Q9NR50) Human eukaryotic initiation factor EIF2B epsilon subunits × 2 (Q13144) C7B 2-(4-chloranylphenoxy)-~{N}-[4-[2-(4-chloranylphenoxy)ethanoylamino]cyclohexyl]ethanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 G; PDBConstruct 1–523; UniProt 1–523 Author chain H; PDBConstruct 1–523; UniProt 1–523

Human eukaryotic initiation factor EIF2B epsilon subunits

OrganismNot specified

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain I; UniProt 1–721 Chain J; UniProt 1–721 Not recorded Translation initiation factor eIF-2B subunit alpha × 2 (Q14232) Translation initiation factor eIF-2B subunit beta × 2 (P49770) Translation initiation factor eIF-2B subunit gamma × 2 (Q9NR50) Translation initiation factor eIF-2B subunit delta × 2 (Q9UI10) C7B 2-(4-chloranylphenoxy)-~{N}-[4-[2-(4-chloranylphenoxy)ethanoylamino]cyclohexyl]ethanamide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 5
Chains and sequence ranges Author chain I; PDBConstruct 1–721; UniProt 1–721 Author chain J; PDBConstruct 1–721; UniProt 1–721

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 6ezo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ezo
Deposition date deposition_date2017-11-16
Structure title titleEukaryotic initiation factor EIF2B in complex with ISRIB
Keywords keywordsGEF, Complex, ISRIB, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.55
Radius of gyration Rg (electron density) rg_electron52.54
Forward intensity I(0) i01253980000.00
Molecular weight molecular_weight262500.0 kDa
Excluded volume excluded_volume313400 ų
Envelope volume envelope_volume615290 ų
Hydration-shell volume shell_volume97969 ų
Envelope diameter envelope_diameter175.3
Shell Rg shell_rg54.95
Envelope Rg envelope_rg52.36
Shape Rg shape_rg52.63
Total Rg total_rg52.38
Total atoms total_atoms18758
Residues n_residues3367
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 dmax170.2
Rg (real space) rg_real53.51
Rg uncertainty (real space) rg_real_error1.34
I(0) (real space) i0_real1.2540e+09
I(0) uncertainty (real space) i0_real_error2.4190e+07
Rg (reciprocal space) rg_reciprocal53.56
I(0) (reciprocal space) i0_reciprocal1254000000.0000
Solution quality estimate total_estimate0.8578
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.7
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha183700000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.363

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)