8qfc

UFL1 E3 ligase bound 60S ribosome

Method: ELECTRON MICROSCOPY Dmax: 222.9 Å Quality: REASONABLE

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

60S ribosomal protein L10a

Homo sapiens

UniProt P62906

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–217 Not recorded E3 UFM1-protein ligase 1 × 1 (O94874) CDK5 regulatory subunit-associated protein 3 × 1 (Q96JB5) DDRGK domain-containing protein 1 × 1 (Q96HY6) Ubiquitin-fold modifier 1 × 1 (A0A8C2YGR4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl2, 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

53 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL10A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–217; UniProt 1–217

E3 UFM1-protein ligase 1

Homo sapiens

UniProt O94874

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–794 Not recorded 60S ribosomal protein L10a × 1 (P62906) CDK5 regulatory subunit-associated protein 3 × 1 (Q96JB5) DDRGK domain-containing protein 1 × 1 (Q96HY6) Ubiquitin-fold modifier 1 × 1 (A0A8C2YGR4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl2, 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFL1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 16–809; UniProt 1–794

CDK5 regulatory subunit-associated protein 3

Homo sapiens

UniProt Q96JB5

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–506 Not recorded 60S ribosomal protein L10a × 1 (P62906) E3 UFM1-protein ligase 1 × 1 (O94874) DDRGK domain-containing protein 1 × 1 (Q96HY6) Ubiquitin-fold modifier 1 × 1 (A0A8C2YGR4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl2, 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CK5P3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–511; UniProt 1–506

DDRGK domain-containing protein 1

Homo sapiens

UniProt Q96HY6

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 29–314 Not recorded 60S ribosomal protein L10a × 1 (P62906) E3 UFM1-protein ligase 1 × 1 (O94874) CDK5 regulatory subunit-associated protein 3 × 1 (Q96JB5) Ubiquitin-fold modifier 1 × 1 (A0A8C2YGR4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl2, 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDRGK_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 18–303; UniProt 29–314

Ubiquitin-fold modifier 1

Homo sapiens

UniProt A0A8C2YGR4

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 112–198 Not recorded 60S ribosomal protein L10a × 1 (P62906) E3 UFM1-protein ligase 1 × 1 (O94874) CDK5 regulatory subunit-associated protein 3 × 1 (Q96JB5) DDRGK domain-containing protein 1 × 1 (Q96HY6) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;25 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl2, 2 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8C2YGR4_COTJA
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–87; UniProt 112–198

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 8qfc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8qfc
Deposition date deposition_date2023-09-04
Structure title titleUFL1 E3 ligase bound 60S ribosome
Keywords keywordsUFM1, Ligase, Ribosome, Complex; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier78.20
Radius of gyration Rg (electron density) rg_electron78.67
Forward intensity I(0) i0331167000.00
Molecular weight molecular_weight155560.0 kDa
Excluded volume excluded_volume195850 ų
Envelope volume envelope_volume446760 ų
Hydration-shell volume shell_volume51187 ų
Envelope diameter envelope_diameter251.6
Shell Rg shell_rg69.03
Envelope Rg envelope_rg74.92
Shape Rg shape_rg78.71
Total Rg total_rg78.30
Total atoms total_atoms10968
Residues n_residues1488
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 dmax222.9
Rg (real space) rg_real78.51
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real3.3060e+08
I(0) uncertainty (real space) i0_real_error6.6890e+06
Rg (reciprocal space) rg_reciprocal75.40
I(0) (reciprocal space) i0_reciprocal328700000.0000
Solution quality estimate total_estimate0.7030
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.213
Kurtosis Kurtosis kurtosis-1.075
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0060
Highest regularization parameter α highest_alpha10170000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.595; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.362; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)