8c0d

UFL1/DDRGK1 bound to UFC1

Method: X-RAY DIFFRACTION Dmax: 183.4 Å Quality: REASONABLE

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–179 Not recorded DDRGK domain-containing protein 1 × 1 (Q96HY6) Ubiquitin-fold modifier-conjugating enzyme 1 × 1 (Q9Y3C8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;292 K;0.1M HEPES, 1.03M Li2SO4 Resolution 2.56 Å R-free 0.286
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–179 Not recorded DDRGK domain-containing protein 1 × 1 (Q96HY6) Ubiquitin-fold modifier-conjugating enzyme 1 × 1 (Q9Y3C8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;292 K;0.1M HEPES, 1.03M Li2SO4 Resolution 2.56 Å R-free 0.286

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 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 16–194; UniProt 1–179 Author chain D; PDBConstruct 16–194; UniProt 1–179

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 205–314 Not recorded E3 UFM1-protein ligase 1 × 1 (O94874) Ubiquitin-fold modifier-conjugating enzyme 1 × 1 (Q9Y3C8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;292 K;0.1M HEPES, 1.03M Li2SO4 Resolution 2.56 Å R-free 0.286
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 205–314 Not recorded E3 UFM1-protein ligase 1 × 1 (O94874) Ubiquitin-fold modifier-conjugating enzyme 1 × 1 (Q9Y3C8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;292 K;0.1M HEPES, 1.03M Li2SO4 Resolution 2.56 Å R-free 0.286

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 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DDRGK_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–110; UniProt 205–314 Author chain E; PDBConstruct 1–110; UniProt 205–314

Ubiquitin-fold modifier-conjugating enzyme 1

Homo sapiens

UniProt Q9Y3C8

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–167 Not recorded E3 UFM1-protein ligase 1 × 1 (O94874) DDRGK domain-containing protein 1 × 1 (Q96HY6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;292 K;0.1M HEPES, 1.03M Li2SO4 Resolution 2.56 Å R-free 0.286
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–167 Not recorded E3 UFM1-protein ligase 1 × 1 (O94874) DDRGK domain-containing protein 1 × 1 (Q96HY6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.2;292 K;0.1M HEPES, 1.03M Li2SO4 Resolution 2.56 Å R-free 0.286

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 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFC1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–167; UniProt 1–167 Author chain F; PDBConstruct 1–167; UniProt 1–167

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 8c0d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8c0d
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8c0d
Deposition date deposition_date2022-12-16
Structure title titleUFL1/DDRGK1 bound to UFC1
Keywords keywordsUFM1, E3 ligase, ubiquitin, UFBP1, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.09
Radius of gyration Rg (electron density) rg_electron43.57
Forward intensity I(0) i0129716000.00
Molecular weight molecular_weight92111.0 kDa
Excluded volume excluded_volume115440 ų
Envelope volume envelope_volume167870 ų
Hydration-shell volume shell_volume37048 ų
Envelope diameter envelope_diameter188.5
Shell Rg shell_rg40.98
Envelope Rg envelope_rg44.27
Shape Rg shape_rg43.57
Total Rg total_rg43.39
Total atoms total_atoms12900
Residues n_residues850
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 dmax183.4
Rg (real space) rg_real46.69
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.3160e+08
I(0) uncertainty (real space) i0_real_error2.4780e+06
Rg (reciprocal space) rg_reciprocal43.09
I(0) (reciprocal space) i0_reciprocal129600000.0000
Solution quality estimate total_estimate0.5238
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.6
Skewness Skewness skewness0.819
Kurtosis Kurtosis kurtosis0.410
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha1.1210
Highest regularization parameter α highest_alpha8433000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.416; Stabil: 0.822; Sysdev: 0.000; Positv: 1.000; Valcen: 0.341; Smooth: 0.787

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)