9gj5

Human 80S ribosome in complex with NatA in distal position and Ebp1

Method: ELECTRON MICROSCOPY Dmax: 217.5 Å Quality: GOOD

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

N-alpha-acetyltransferase 10

Homo sapiens

UniProt P41227

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain 2; UniProt 2–170 Not recorded 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NAA10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain 2; PDBConstruct 3–171; UniProt 2–170

N-alpha-acetyltransferase 15, NatA auxiliary subunit

Homo sapiens

UniProt Q9BXJ9

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain B; UniProt 1–841 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NAA15_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–840; UniProt 1–841

60S ribosomal protein L4

Homo sapiens

UniProt P36578

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain LC; UniProt 1–427 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

178 other PDB entries and 178 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL4_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain LC; PDBConstruct 1–427; UniProt 1–427

Large ribosomal subunit protein eL6

Homo sapiens

UniProt Q02878

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain LE; UniProt 1–288 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

176 other PDB entries and 176 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL6_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain LE; PDBConstruct 1–288; UniProt 1–288

60S ribosomal protein L38

Homo sapiens

UniProt P63173

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Lk; UniProt 1–70 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

167 other PDB entries and 167 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL38_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain Lk; PDBConstruct 1–70; UniProt 1–70

Large ribosomal subunit protein uL24

Homo sapiens

UniProt P61254

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain LY; UniProt 1–145 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

176 other PDB entries and 176 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL26_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain LY; PDBConstruct 1–144; UniProt 1–145

60S ribosomal protein L35

Homo sapiens

UniProt P42766

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Lh; UniProt 2–123 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

177 other PDB entries and 177 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL35_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain Lh; PDBConstruct 1–122; UniProt 2–123

60S ribosomal protein L23a

Homo sapiens

UniProt P62750

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain LX; UniProt 1–156 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

177 other PDB entries and 177 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL23A_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain LX; PDBConstruct 1–156; UniProt 1–156

60S ribosomal protein L19

Homo sapiens

UniProt P84098

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain LR; UniProt 1–196 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L28 × 1 (P46779) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

169 other PDB entries and 169 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL19_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain LR; PDBConstruct 1–196; UniProt 1–196

60S ribosomal protein L28

Homo sapiens

UniProt P46779

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain Lr; UniProt 1–137 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) Proliferation-associated protein 2G4 × 1 (Q9UQ80) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

171 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL28_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain Lr; PDBConstruct 1–137; UniProt 1–137

Proliferation-associated protein 2G4

Homo sapiens

UniProt Q9UQ80

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 × 11 RNA 2 PDB declaration: 13-meric(13) Consistent with all polymer counts Chain A; UniProt 1–394 Not recorded N-alpha-acetyltransferase 10 × 1 (P41227) 5.8S rRNA × 1 N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 (Q9BXJ9) 28S rRNA × 1 60S ribosomal protein L4 × 1 (P36578) Large ribosomal subunit protein eL6 × 1 (Q02878) 60S ribosomal protein L38 × 1 (P63173) Large ribosomal subunit protein uL24 × 1 (P61254) 60S ribosomal protein L35 × 1 (P42766) 60S ribosomal protein L23a × 1 (P62750) 60S ribosomal protein L19 × 1 (P84098) 60S ribosomal protein L28 × 1 (P46779) KGN D-chiro inositol hexakisphosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.61 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.

30 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PA2G4_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain A; PDBConstruct 1–394; UniProt 1–394

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 9gj5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gj5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gj5
Deposition date deposition_date2024-08-21
Structure title titleHuman 80S ribosome in complex with NatA in distal position and Ebp1
Keywords keywordshuman 80S ribosome, N-terminal acetylation (NTA), N-acety-transferase A (NatA), Ebp1, PA2G4, TRANSLATION; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.05
Radius of gyration Rg (electron density) rg_electron68.57
Forward intensity I(0) i03712830000.00
Molecular weight molecular_weight426170.0 kDa
Excluded volume excluded_volume498650 ų
Envelope volume envelope_volume989190 ų
Hydration-shell volume shell_volume124630 ų
Envelope diameter envelope_diameter247.0
Shell Rg shell_rg63.58
Envelope Rg envelope_rg69.06
Shape Rg shape_rg68.52
Total Rg total_rg68.61
Total atoms total_atoms29428
Residues n_residues3030
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 dmax217.5
Rg (real space) rg_real68.17
Rg uncertainty (real space) rg_real_error1.29
I(0) (real space) i0_real3.7110e+09
I(0) uncertainty (real space) i0_real_error6.7760e+07
Rg (reciprocal space) rg_reciprocal67.33
I(0) (reciprocal space) i0_reciprocal3707000000.0000
Solution quality estimate total_estimate0.8489
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.7
Skewness Skewness skewness0.450
Kurtosis Kurtosis kurtosis-0.251
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0179
Highest regularization parameter α highest_alpha137300000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.203

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)