4zgq

Structure of Cdc123 bound to eIF2-gammaDIII domain

Method: X-RAY DIFFRACTION Dmax: 86.0 Å Quality: GOOD

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

Cell division cycle protein 123

Schizosaccharomyces pombe

UniProt Q9P7N5

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 1–319 Not recorded Eukaryotic translation initiation factor 2 subunit gamma × 1 (P32481) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;298 K;25%PEG3350, 0.2M LISO4, 0.1M Tris pH 8.0 Resolution 3.00 Å R-free 0.252

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 CD123_SCHPO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 20–338; UniProt 1–319

Eukaryotic translation initiation factor 2 subunit gamma

Saccharomyces cerevisiae

UniProt P32481

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 410–527 Fragment:UNP residues 410-527 Cell division cycle protein 123 × 1 (Q9P7N5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;298 K;25%PEG3350, 0.2M LISO4, 0.1M Tris pH 8.0 Resolution 3.00 Å R-free 0.252

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.

24 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IF2G_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–118; UniProt 410–527

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 4zgq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4zgq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4zgq
Deposition date deposition_date2015-04-23
Structure title titleStructure of Cdc123 bound to eIF2-gammaDIII domain
Keywords keywordsATP-grasp fold, cell cycle, eIF2; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.36
Radius of gyration Rg (electron density) rg_electron24.41
Forward intensity I(0) i028697700.00
Molecular weight molecular_weight42956.0 kDa
Excluded volume excluded_volume54584 ų
Envelope volume envelope_volume71381 ų
Hydration-shell volume shell_volume24610 ų
Envelope diameter envelope_diameter89.1
Shell Rg shell_rg31.16
Envelope Rg envelope_rg25.25
Shape Rg shape_rg24.38
Total Rg total_rg25.39
Total atoms total_atoms3032
Residues n_residues374
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 dmax86.0
Rg (real space) rg_real25.40
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.8700e+07
I(0) uncertainty (real space) i0_real_error4.7230e+05
Rg (reciprocal space) rg_reciprocal25.38
I(0) (reciprocal space) i0_reciprocal28700000.0000
Solution quality estimate total_estimate0.8782
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.394
Kurtosis Kurtosis kurtosis-0.294
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5998000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4zgqB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors

8. Citations (1)

9. Files and Curves (10)