12fh

Structure of eIF2B bound to a activator

Method: X-RAY DIFFRACTION Dmax: 118.8 Å Quality: GOOD

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

Isoform 2 of Translation initiation factor eIF2B 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 2–543 Chain B; UniProt 2–543 Non-standard monomer:Yes (specific site not provided by mmCIF) Translation initiation factor eIF2B subunit beta × 2 (P49770) unidentified protein fragment × 1 SULFATE ION × 2 N,N'-[(1S,2S,4R)-2-hydroxybicyclo[2.2.2]octane-1,4-diyl]bis[2-(4-chloro-3-fluorophenoxy)acetamide] × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.50 Å R-free 0.271

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 Q9UI10-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–542; UniProt 2–543 Author chain B; PDBConstruct 1–542; UniProt 2–543

Translation initiation factor eIF2B 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–351 Chain D; UniProt 1–351 Non-standard monomer:Yes (specific site not provided by mmCIF) Isoform 2 of Translation initiation factor eIF2B subunit delta × 2 (Q9UI10) unidentified protein fragment × 1 SULFATE ION × 2 N,N'-[(1S,2S,4R)-2-hydroxybicyclo[2.2.2]octane-1,4-diyl]bis[2-(4-chloro-3-fluorophenoxy)acetamide] × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.50 Å R-free 0.271

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 16–366; UniProt 1–351 Author chain D; PDBConstruct 16–366; UniProt 1–351

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 12fh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 12fh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id12fh
Deposition date deposition_date2026-04-01
最后修订 last_revision2026-06-03
Structure title titleStructure of eIF2B bound to a activator
Keywords keywordsguanine nucleotide exchange factor, translation initiation, protein complex, SUGAR BINDING PROTEIN; SUGAR BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.64
Radius of gyration Rg (electron density) rg_electron36.10
Forward intensity I(0) i0675686000.00
Molecular weight molecular_weight139390.0 kDa
Excluded volume excluded_volume133870 ų
Envelope volume envelope_volume241990 ų
Hydration-shell volume shell_volume54841 ų
Envelope diameter envelope_diameter127.5
Shell Rg shell_rg42.95
Envelope Rg envelope_rg36.51
Shape Rg shape_rg36.11
Total Rg total_rg36.40
Total atoms total_atoms10538
Residues n_residues1342
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 dmax118.8
Rg (real space) rg_real36.60
Rg uncertainty (real space) rg_real_error0.99
I(0) (real space) i0_real6.7570e+08
I(0) uncertainty (real space) i0_real_error1.1070e+07
Rg (reciprocal space) rg_reciprocal36.63
I(0) (reciprocal space) i0_reciprocal675700000.0000
Solution quality estimate total_estimate0.8841
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.2
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.261
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61220000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.799

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)