8phd

Structure of Human Cdc123 bound to domain 3 of eIF2 gamma and ATP

Method: X-RAY DIFFRACTION Dmax: 107.4 Å Quality: EXCELLENT

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

Cell division cycle protein 123 homolog

Homo sapiens

UniProt O75794

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–336 Not recorded Eukaryotic translation initiation factor 2 subunit 3 × 1 (P41091) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20% PEG3350 0.2 M lithium citrate 1 mM ATP 5 mM MgCl2 Resolution 2.08 Å R-free 0.205
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–336 Not recorded Eukaryotic translation initiation factor 2 subunit 3 × 1 (P41091) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20% PEG3350 0.2 M lithium citrate 1 mM ATP 5 mM MgCl2 Resolution 2.08 Å R-free 0.205

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD123_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–356; UniProt 1–336 Author chain C; PDBConstruct 21–356; UniProt 1–336

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 363–472 Not recorded Cell division cycle protein 123 homolog × 1 (O75794) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20% PEG3350 0.2 M lithium citrate 1 mM ATP 5 mM MgCl2 Resolution 2.08 Å R-free 0.205
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 363–472 Not recorded Cell division cycle protein 123 homolog × 1 (O75794) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20% PEG3350 0.2 M lithium citrate 1 mM ATP 5 mM MgCl2 Resolution 2.08 Å R-free 0.205

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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2G_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–111; UniProt 363–472 Author chain D; PDBConstruct 2–111; UniProt 363–472

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 8phd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8phd
Deposition date deposition_date2023-06-19
Structure title titleStructure of Human Cdc123 bound to domain 3 of eIF2 gamma and ATP
Keywords keywordseIF2, translation initiation, chaperone, Cdc123, ATP grasp, TRANSLATION; TRANSLATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.11
Radius of gyration Rg (electron density) rg_electron33.50
Forward intensity I(0) i0132365000.00
Molecular weight molecular_weight93137.0 kDa
Excluded volume excluded_volume117140 ų
Envelope volume envelope_volume161840 ų
Hydration-shell volume shell_volume40235 ų
Envelope diameter envelope_diameter109.0
Shell Rg shell_rg40.63
Envelope Rg envelope_rg32.31
Shape Rg shape_rg33.48
Total Rg total_rg34.20
Total atoms total_atoms6569
Residues n_residues795
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 dmax107.4
Rg (real space) rg_real34.00
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real1.3240e+08
I(0) uncertainty (real space) i0_real_error2.0380e+06
Rg (reciprocal space) rg_reciprocal34.07
I(0) (reciprocal space) i0_reciprocal132400000.0000
Solution quality estimate total_estimate0.9059
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary49.0
Skewness Skewness skewness0.107
Kurtosis Kurtosis kurtosis-0.693
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52700000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)