9x4h

Structure Of the KEOPS-tRNA

Method: ELECTRON MICROSCOPY Dmax: 139.6 Å Quality: REASONABLE

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–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain A; UniProt 1–337 Chain F; UniProt 1–337 Not recorded non-specific serine/threonine protein kinase × 1 (B5WWL2) EKC/KEOPS complex subunit TPRKB × 1 (O44566) L antigen family member 3 × 2 (Q21019) RNA (76-MER) × 1 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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 F; 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–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain B; UniProt 1–245 Not recorded N(6)-L-threonylcarbamoyladenine synthase × 2 (Q9BL28) EKC/KEOPS complex subunit TPRKB × 1 (O44566) L antigen family member 3 × 2 (Q21019) RNA (76-MER) × 1 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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

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–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain C; UniProt 1–183 Not recorded N(6)-L-threonylcarbamoyladenine synthase × 2 (Q9BL28) non-specific serine/threonine protein kinase × 1 (B5WWL2) L antigen family member 3 × 2 (Q21019) RNA (76-MER) × 1 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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

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–RNA Heteromer Protein × 6 RNA 1 PDB declaration: heptameric(7) Consistent with all polymer counts Chain D; UniProt 1–123 Chain E; UniProt 1–123 Not recorded N(6)-L-threonylcarbamoyladenine synthase × 2 (Q9BL28) non-specific serine/threonine protein kinase × 1 (B5WWL2) EKC/KEOPS complex subunit TPRKB × 1 (O44566) RNA (76-MER) × 1 K POTASSIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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 E; 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 9x4h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9x4h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9x4h
Deposition date deposition_date2025-10-10
Structure title titleStructure Of the KEOPS-tRNA
Keywords keywords;tRNA modification, t6A, KEOPS-tRNA complex, cryo-EM structure, substrate recognition, catalytic mechanism, regulation principle, TRANSFERASE/RNA, TRANSFERASE-RNA complex ;; TRANSFERASE/RNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.14
Radius of gyration Rg (electron density) rg_electron40.55
Forward intensity I(0) i0400330000.00
Molecular weight molecular_weight146020.0 kDa
Excluded volume excluded_volume175770 ų
Envelope volume envelope_volume242790 ų
Hydration-shell volume shell_volume52434 ų
Envelope diameter envelope_diameter152.5
Shell Rg shell_rg43.54
Envelope Rg envelope_rg40.44
Shape Rg shape_rg40.56
Total Rg total_rg40.65
Total atoms total_atoms10131
Residues n_residues1178
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 dmax139.6
Rg (real space) rg_real39.46
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real4.0030e+08
I(0) uncertainty (real space) i0_real_error6.9180e+06
Rg (reciprocal space) rg_reciprocal39.26
I(0) (reciprocal space) i0_reciprocal400200000.0000
Solution quality estimate total_estimate0.6246
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.554
Kurtosis Kurtosis kurtosis-0.028
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37500000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 0.062; Positv: 1.000; Valcen: 0.876; Smooth: 0.804

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)