9gj6

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

Method: ELECTRON MICROSCOPY Dmax: 258.6 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain A; UniProt 1–235 Chain C; UniProt 1–235 Not recorded N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 A; PDBConstruct 1–235; UniProt 1–235 Author chain C; PDBConstruct 1–235; UniProt 1–235

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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain B; UniProt 1–841 Chain D; UniProt 1–841 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–840; UniProt 1–841 Author chain D; 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LC; UniProt 1–427 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LE; UniProt 1–288 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain Lk; UniProt 1–70 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LY; UniProt 1–145 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 1–145; 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain Lh; UniProt 2–123 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LX; UniProt 1–156 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LR; UniProt 1–196 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain Lr; UniProt 1–137 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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

Large ribosomal subunit protein eL22

Homo sapiens

UniProt P35268

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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LU; UniProt 2–128 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) 60S ribosomal protein L31 × 1 (P62899) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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.

125 other PDB entries and 125 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL22_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain LU; PDBConstruct 1–127; UniProt 2–128

60S ribosomal protein L31

Homo sapiens

UniProt P62899

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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain Ld; UniProt 1–125 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L17 × 1 (P18621) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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.

164 other PDB entries and 164 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL31_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain Ld; PDBConstruct 1–125; UniProt 1–125

60S ribosomal protein L17

Homo sapiens

UniProt P18621

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 × 15 RNA 2 PDB declaration: 17-meric(17) Consistent with all polymer counts Chain LP; UniProt 1–184 Not recorded N-alpha-acetyltransferase 10 × 2 (P41227) N-alpha-acetyltransferase 15, NatA auxiliary subunit × 2 (Q9BXJ9) 28S rRNA × 1 5.8S 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) Large ribosomal subunit protein eL22 × 1 (P35268) 60S ribosomal protein L31 × 1 (P62899) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.91 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.

174 other PDB entries and 174 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL17_HUMAN
Isoform
PDB entities 15
Chains and sequence ranges Author chain LP; PDBConstruct 1–184; UniProt 1–184

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 9gj6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gj6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gj6
Deposition date deposition_date2024-08-21
Structure title titleHuman 80S ribosome in complex with NatA in proximal and distal position
Keywords keywordshuman 80S ribosome, N-terminal acetylation (NTA), N-acety-transferase A (NatA) in proximal and distal position, TRANSLATION; TRANSLATION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.75
Radius of gyration Rg (electron density) rg_electron73.91
Forward intensity I(0) i08429330000.00
Molecular weight molecular_weight628520.0 kDa
Excluded volume excluded_volume726040 ų
Envelope volume envelope_volume1456800 ų
Hydration-shell volume shell_volume164690 ų
Envelope diameter envelope_diameter248.2
Shell Rg shell_rg73.64
Envelope Rg envelope_rg71.16
Shape Rg shape_rg73.83
Total Rg total_rg74.10
Total atoms total_atoms43288
Residues n_residues4294
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 dmax258.6
Rg (real space) rg_real74.56
Rg uncertainty (real space) rg_real_error2.73
I(0) (real space) i0_real8.4290e+09
I(0) uncertainty (real space) i0_real_error2.0320e+08
Rg (reciprocal space) rg_reciprocal75.25
I(0) (reciprocal space) i0_reciprocal8440000000.0000
Solution quality estimate total_estimate0.8671
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary98.5
Skewness Skewness skewness0.154
Kurtosis Kurtosis kurtosis-0.499
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha258800000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.785

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)