9x4g

Structure Of the KEOPS dimer

Method: ELECTRON MICROSCOPY Dmax: 162.3 Å Quality: GOOD

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

N(6)-L-threonylcarbamoyladenine synthase

Caenorhabditis elegans

UniProt Q9BL28

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–337 Chain E; UniProt 1–337 Not recorded non-specific serine/threonine protein kinase × 2 (B5WWL2) EKC/KEOPS complex subunit TPRKB × 2 (O44566) L antigen family member 3 × 2 (Q21019) K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name Q9BL28_CAEEL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–337; UniProt 1–337 Author chain E; PDBConstruct 1–337; UniProt 1–337

non-specific serine/threonine protein kinase

Caenorhabditis elegans

UniProt B5WWL2

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–245 Chain F; UniProt 1–245 Not recorded N(6)-L-threonylcarbamoyladenine synthase × 2 (Q9BL28) EKC/KEOPS complex subunit TPRKB × 2 (O44566) L antigen family member 3 × 2 (Q21019) K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name B5WWL2_CAEEL
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–245; UniProt 1–245 Author chain F; PDBConstruct 1–245; UniProt 1–245

EKC/KEOPS complex subunit TPRKB

Caenorhabditis elegans

UniProt O44566

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–183 Chain G; UniProt 1–183 Not recorded N(6)-L-threonylcarbamoyladenine synthase × 2 (Q9BL28) non-specific serine/threonine protein kinase × 2 (B5WWL2) L antigen family member 3 × 2 (Q21019) K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name O44566_CAEEL
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–183; UniProt 1–183 Author chain G; PDBConstruct 1–183; UniProt 1–183

L antigen family member 3

Caenorhabditis elegans

UniProt Q21019

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 1–123 Chain H; UniProt 1–123 Not recorded N(6)-L-threonylcarbamoyladenine synthase × 2 (Q9BL28) non-specific serine/threonine protein kinase × 2 (B5WWL2) EKC/KEOPS complex subunit TPRKB × 2 (O44566) K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name Q21019_CAEEL
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–123; UniProt 1–123 Author chain H; PDBConstruct 1–123; UniProt 1–123

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 9x4g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x4g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x4g
Deposition date deposition_date2025-10-10
Structure title titleStructure Of the KEOPS dimer
Keywords keywords;tRNA modification, t6A, KEOPS-tRNA complex, cryo-EM structure, substrate recognition, catalytic mechanism, regulation principle, TRANSFERASE ;; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.88
Radius of gyration Rg (electron density) rg_electron50.90
Forward intensity I(0) i0402877000.00
Molecular weight molecular_weight167740.0 kDa
Excluded volume excluded_volume211130 ų
Envelope volume envelope_volume309120 ų
Hydration-shell volume shell_volume52896 ų
Envelope diameter envelope_diameter175.1
Shell Rg shell_rg50.61
Envelope Rg envelope_rg50.68
Shape Rg shape_rg50.92
Total Rg total_rg50.85
Total atoms total_atoms11768
Residues n_residues1518
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 dmax162.3
Rg (real space) rg_real50.48
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real4.0290e+08
I(0) uncertainty (real space) i0_real_error8.5510e+06
Rg (reciprocal space) rg_reciprocal49.89
I(0) (reciprocal space) i0_reciprocal402600000.0000
Solution quality estimate total_estimate0.8067
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.7
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis-0.507
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19230000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.802; Smooth: 0.054

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)