6ybv

Structure of a human 48S translational initiation complex - eIF2-TC

Method: ELECTRON MICROSCOPY Dmax: 120.0 Å Quality: EXCELLENT

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

Eukaryotic translation initiation factor 2 subunit 2

OrganismNot specified

UniProt P20042

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–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain s; UniProt 1–333 Not recorded Eukaryotic translation initiation factor 2 subunit 1 × 1 (P05198) Initiator methionine tRNA × 1 mRNA × 1 Eukaryotic translation initiation factor 2 subunit 3 × 1 (P41091) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain s; PDBConstruct 1–333; UniProt 1–333

Eukaryotic translation initiation factor 2 subunit 1

OrganismNot specified

UniProt P05198

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–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain r; UniProt 1–315 Not recorded Eukaryotic translation initiation factor 2 subunit 2 × 1 (P20042) Initiator methionine tRNA × 1 mRNA × 1 Eukaryotic translation initiation factor 2 subunit 3 × 1 (P41091) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

36 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2A_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain r; PDBConstruct 1–315; UniProt 1–315

Eukaryotic translation initiation factor 2 subunit 3

OrganismNot specified

UniProt P41091

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–RNA Heteromer Protein × 3 RNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain t; UniProt 1–472 Not recorded Eukaryotic translation initiation factor 2 subunit 2 × 1 (P20042) Eukaryotic translation initiation factor 2 subunit 1 × 1 (P05198) Initiator methionine tRNA × 1 mRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2G_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain t; PDBConstruct 1–472; UniProt 1–472

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 6ybv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ybv
Deposition date deposition_date2020-03-17
Structure title titleStructure of a human 48S translational initiation complex - eIF2-TC
Keywords keywordsribosome, translation, initiation complex; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.20
Radius of gyration Rg (electron density) rg_electron37.73
Forward intensity I(0) i0225183000.00
Molecular weight molecular_weight97010.0 kDa
Excluded volume excluded_volume111090 ų
Envelope volume envelope_volume192230 ų
Hydration-shell volume shell_volume42802 ų
Envelope diameter envelope_diameter125.9
Shell Rg shell_rg43.43
Envelope Rg envelope_rg36.86
Shape Rg shape_rg37.83
Total Rg total_rg37.84
Total atoms total_atoms6731
Residues n_residues847
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 dmax120.0
Rg (real space) rg_real37.22
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real2.2520e+08
I(0) uncertainty (real space) i0_real_error3.4890e+06
Rg (reciprocal space) rg_reciprocal37.21
I(0) (reciprocal space) i0_reciprocal225200000.0000
Solution quality estimate total_estimate0.9002
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.1
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.655
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12840000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.948; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.902

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id6ybvr01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily140 — Nucleic acid-binding proteins
Domain ID domain_id6ybvr02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily190 — Translation initiation factor 2; subunit 1; domain 2
Domain ID domain_id6ybvr03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1130 — EIF_2_alpha

8. Citations (1)

9. Files and Curves (10)