8qzz

Crystal structure of human eIF2 alpha-gamma complexed with PPP1R15A_420-452

Method: X-RAY DIFFRACTION Dmax: 92.7 Å Quality: REASONABLE

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

Eukaryotic translation initiation factor 2 subunit 3

Homo sapiens

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–472 Not recorded Eukaryotic translation initiation factor 2 subunit 1 × 1 (P05198) Protein phosphatase 1 regulatory subunit 15A × 1 (O75807) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;11-12% PEG 6000, 0.1M Tris-HCl pH8.5 supplemented with amino acids Resolution 3.35 Å R-free 0.299

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–472; UniProt 1–472

Eukaryotic translation initiation factor 2 subunit 1

Homo sapiens

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–315 Not recorded Eukaryotic translation initiation factor 2 subunit 3 × 1 (P41091) Protein phosphatase 1 regulatory subunit 15A × 1 (O75807) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;11-12% PEG 6000, 0.1M Tris-HCl pH8.5 supplemented with amino acids Resolution 3.35 Å R-free 0.299

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 B; PDBConstruct 1–315; UniProt 1–315

Protein phosphatase 1 regulatory subunit 15A

Homo sapiens

UniProt O75807

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 420–452 Not recorded Eukaryotic translation initiation factor 2 subunit 3 × 1 (P41091) Eukaryotic translation initiation factor 2 subunit 1 × 1 (P05198) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;11-12% PEG 6000, 0.1M Tris-HCl pH8.5 supplemented with amino acids Resolution 3.35 Å R-free 0.299

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PR15A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–33; UniProt 420–452

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 8qzz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qzz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qzz
Deposition date deposition_date2023-10-30
Structure title titleCrystal structure of human eIF2 alpha-gamma complexed with PPP1R15A_420-452
Keywords keywordsEukaryotic Initiation Factor-2, PP1 regulatory subunit, dephosphorylation, metabolism, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.30
Radius of gyration Rg (electron density) rg_electron27.59
Forward intensity I(0) i057918000.00
Molecular weight molecular_weight60102.0 kDa
Excluded volume excluded_volume75702 ų
Envelope volume envelope_volume96338 ų
Hydration-shell volume shell_volume29714 ų
Envelope diameter envelope_diameter97.3
Shell Rg shell_rg34.06
Envelope Rg envelope_rg27.88
Shape Rg shape_rg27.57
Total Rg total_rg28.33
Total atoms total_atoms4213
Residues n_residues555
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 dmax92.7
Rg (real space) rg_real28.32
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real5.7920e+07
I(0) uncertainty (real space) i0_real_error7.5900e+05
Rg (reciprocal space) rg_reciprocal28.32
I(0) (reciprocal space) i0_reciprocal57920000.0000
Solution quality estimate total_estimate0.7196
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis-0.362
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11030000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.973; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)