7nvk

Crystal structure of UBA5 fragment fused to the N-terminus of UFC1

Method: X-RAY DIFFRACTION Dmax: 78.5 Å Quality: GOOD

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

Ubiquitin-like modifier-activating enzyme 5,Ubiquitin-fold modifier-conjugating enzyme 1

Homo sapiens

UniProt Q9GZZ9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain AAA; UniProt 347–404 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;2% (v/v) Tacsimate pH 7.0, 20% PEG 3350, 0.1M HEPES pH 7.5, 6mM zinc sulfate Resolution 2.65 Å R-free 0.264

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.

9 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBA5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 2–59; UniProt 347–404

Ubiquitin-like modifier-activating enzyme 5,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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain AAA; UniProt 1–167 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;2% (v/v) Tacsimate pH 7.0, 20% PEG 3350, 0.1M HEPES pH 7.5, 6mM zinc sulfate Resolution 2.65 Å R-free 0.264

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UFC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 60–226; 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 7nvk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nvk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7nvk
Deposition date deposition_date2021-03-15
Structure title titleCrystal structure of UBA5 fragment fused to the N-terminus of UFC1
Keywords keywords;Ubiquitin like fold modifier enzyme 5 (UBA5), E1, Ubiquitin fold modifier 1 (UFM1), Ubiquitin fold modifier conjugating enzyme 1 (UFC1), UFMYLATION, LIGASE ;; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.72
Radius of gyration Rg (electron density) rg_electron19.93
Forward intensity I(0) i08024160.00
Molecular weight molecular_weight21121.0 kDa
Excluded volume excluded_volume26641 ų
Envelope volume envelope_volume33931 ų
Hydration-shell volume shell_volume15610 ų
Envelope diameter envelope_diameter79.2
Shell Rg shell_rg24.35
Envelope Rg envelope_rg21.49
Shape Rg shape_rg19.85
Total Rg total_rg20.95
Total atoms total_atoms1488
Residues n_residues183
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 dmax78.5
Rg (real space) rg_real20.93
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real8.0240e+06
I(0) uncertainty (real space) i0_real_error1.1360e+05
Rg (reciprocal space) rg_reciprocal20.89
I(0) (reciprocal space) i0_reciprocal8024000.0000
Solution quality estimate total_estimate0.7755
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.667
Kurtosis Kurtosis kurtosis0.190
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1252000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.468; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.679; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)