8onz

Chaetomium thermophilum Methionine Aminopeptidase 2 at the 80S ribosome

Method: ELECTRON MICROSCOPY Dmax: 178.0 Å Quality: GOOD

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

Ribosomal protein L19

Thermochaetoides thermophila DSM 1495

UniProt G0S9T3

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 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain LR; UniProt 1–2898 Not recorded 60S ribosomal protein L25-like protein × 1 (G0S507) 60S ribosomal protein L26-like protein × 1 (G0RYN9) dolichyl-diphosphooligosaccharide--protein glycotransferase × 1 (G0S0D7) 60S ribosomal protein L38-like protein × 1 (G0SG89) 28S rRNA × 1 5.8S rRNA × 1 Methionine aminopeptidase 2 × 1 (G0SEA9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S9T3_CHATD
Isoform
PDB entities 1
Chains and sequence ranges Author chain LR; PDBConstruct 1–2898; UniProt 1–2898

60S ribosomal protein L25-like protein

Thermochaetoides thermophila DSM 1495

UniProt G0S507

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 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain LX; UniProt 1–156 Not recorded Ribosomal protein L19 × 1 (G0S9T3) 60S ribosomal protein L26-like protein × 1 (G0RYN9) dolichyl-diphosphooligosaccharide--protein glycotransferase × 1 (G0S0D7) 60S ribosomal protein L38-like protein × 1 (G0SG89) 28S rRNA × 1 5.8S rRNA × 1 Methionine aminopeptidase 2 × 1 (G0SEA9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S507_CHATD
Isoform
PDB entities 2
Chains and sequence ranges Author chain LX; PDBConstruct 1–156; UniProt 1–156

60S ribosomal protein L26-like protein

Thermochaetoides thermophila DSM 1495

UniProt G0RYN9

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 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain LY; UniProt 1–138 Not recorded Ribosomal protein L19 × 1 (G0S9T3) 60S ribosomal protein L25-like protein × 1 (G0S507) dolichyl-diphosphooligosaccharide--protein glycotransferase × 1 (G0S0D7) 60S ribosomal protein L38-like protein × 1 (G0SG89) 28S rRNA × 1 5.8S rRNA × 1 Methionine aminopeptidase 2 × 1 (G0SEA9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0RYN9_CHATD
Isoform
PDB entities 3
Chains and sequence ranges Author chain LY; PDBConstruct 1–138; UniProt 1–138

dolichyl-diphosphooligosaccharide--protein glycotransferase

Thermochaetoides thermophila DSM 1495

UniProt G0S0D7

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 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain Lh; UniProt 1–935 Not recorded Ribosomal protein L19 × 1 (G0S9T3) 60S ribosomal protein L25-like protein × 1 (G0S507) 60S ribosomal protein L26-like protein × 1 (G0RYN9) 60S ribosomal protein L38-like protein × 1 (G0SG89) 28S rRNA × 1 5.8S rRNA × 1 Methionine aminopeptidase 2 × 1 (G0SEA9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

26 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0S0D7_CHATD
Isoform
PDB entities 4
Chains and sequence ranges Author chain Lh; PDBConstruct 1–935; UniProt 1–935

60S ribosomal protein L38-like protein

Thermochaetoides thermophila DSM 1495

UniProt G0SG89

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 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain Lk; UniProt 1–94 Not recorded Ribosomal protein L19 × 1 (G0S9T3) 60S ribosomal protein L25-like protein × 1 (G0S507) 60S ribosomal protein L26-like protein × 1 (G0RYN9) dolichyl-diphosphooligosaccharide--protein glycotransferase × 1 (G0S0D7) 28S rRNA × 1 5.8S rRNA × 1 Methionine aminopeptidase 2 × 1 (G0SEA9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SG89_CHATD
Isoform
PDB entities 5
Chains and sequence ranges Author chain Lk; PDBConstruct 1–94; UniProt 1–94

Methionine aminopeptidase 2

Thermochaetoides thermophila DSM 1495

UniProt G0SEA9

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 2 PDB declaration: octameric(8) Consistent with all polymer counts Chain A; UniProt 1–444 Not recorded Ribosomal protein L19 × 1 (G0S9T3) 60S ribosomal protein L25-like protein × 1 (G0S507) 60S ribosomal protein L26-like protein × 1 (G0RYN9) dolichyl-diphosphooligosaccharide--protein glycotransferase × 1 (G0S0D7) 60S ribosomal protein L38-like protein × 1 (G0SG89) 28S rRNA × 1 5.8S rRNA × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.94 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0SEA9_CHATD
Isoform
PDB entities 8
Chains and sequence ranges Author chain A; PDBConstruct 1–444; UniProt 1–444

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 8onz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8onz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8onz
Deposition date deposition_date2023-04-04
最后修订 last_revision2024-02-21
Structure title titleChaetomium thermophilum Methionine Aminopeptidase 2 at the 80S ribosome
Keywords keywords;Ribosome Associated Factor, Protease, Tunnel exit, Protein Maturation, Proteostasis, NME, p67, MAP, MetAP, MAP2, MetAP2, ES27L, PTE, METAL BINDING PROTEIN ;; METAL BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.06
Radius of gyration Rg (electron density) rg_electron52.91
Forward intensity I(0) i01301790000.00
Molecular weight molecular_weight219620.0 kDa
Excluded volume excluded_volume241960 ų
Envelope volume envelope_volume464850 ų
Hydration-shell volume shell_volume77045 ų
Envelope diameter envelope_diameter201.6
Shell Rg shell_rg51.88
Envelope Rg envelope_rg52.70
Shape Rg shape_rg52.87
Total Rg total_rg52.97
Total atoms total_atoms14990
Residues n_residues1320
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 dmax178.0
Rg (real space) rg_real53.19
Rg uncertainty (real space) rg_real_error2.05
I(0) (real space) i0_real1.3020e+09
I(0) uncertainty (real space) i0_real_error2.6640e+07
Rg (reciprocal space) rg_reciprocal52.93
I(0) (reciprocal space) i0_reciprocal1301000000.0000
Solution quality estimate total_estimate0.8140
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.4
Skewness Skewness skewness0.372
Kurtosis Kurtosis kurtosis-0.442
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35450000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)