9o4m

Crystal structure of Ubiquitin Carboxy Terminal Hydrolase L1 Q209C mutant covalently crosslinked to ubiquitin genetically encoded with N6-(6-bromohexanoyl)-L-lysine

Method: X-RAY DIFFRACTION Dmax: 85.0 Å Quality: EXCELLENT

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

Polyubiquitin-C

Homo sapiens

UniProt P0CG48

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–76 Not recorded Ubiquitin carboxyl-terminal hydrolase isozyme L1 × 1 (P09936) 6NA HEXANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;2.1 M DL-Malic acid Resolution 2.00 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–76 Not recorded Ubiquitin carboxyl-terminal hydrolase isozyme L1 × 1 (P09936) 6NA HEXANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;2.1 M DL-Malic acid Resolution 2.00 Å R-free 0.262

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.

219 other PDB entries and 347 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–76; UniProt 1–76 Author chain D; PDBConstruct 1–76; UniProt 1–76

Ubiquitin carboxyl-terminal hydrolase isozyme L1

Homo sapiens

UniProt P09936

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–223 Mutation:Q209C Polyubiquitin-C × 1 (P0CG48) 6NA HEXANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;2.1 M DL-Malic acid Resolution 2.00 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–223 Mutation:Q209C Polyubiquitin-C × 1 (P0CG48) 6NA HEXANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;2.1 M DL-Malic acid Resolution 2.00 Å R-free 0.262

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.

13 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCHL1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–223; UniProt 1–223 Author chain B; PDBConstruct 1–223; UniProt 1–223

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 9o4m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o4m
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9o4m
Deposition date deposition_date2025-04-08
Structure title titleCrystal structure of Ubiquitin Carboxy Terminal Hydrolase L1 Q209C mutant covalently crosslinked to ubiquitin genetically encoded with N6-(6-bromohexanoyl)-L-lysine
Keywords keywordsUCHL1, genetic code expansion, covalent trapping, unnatural amino acid, ubiquitin, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.41
Radius of gyration Rg (electron density) rg_electron26.45
Forward intensity I(0) i067082200.00
Molecular weight molecular_weight64008.0 kDa
Excluded volume excluded_volume80208 ų
Envelope volume envelope_volume96617 ų
Hydration-shell volume shell_volume30690 ų
Envelope diameter envelope_diameter89.2
Shell Rg shell_rg33.50
Envelope Rg envelope_rg26.51
Shape Rg shape_rg26.44
Total Rg total_rg27.24
Total atoms total_atoms4516
Residues n_residues586
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 dmax85.0
Rg (real space) rg_real27.38
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real6.7080e+07
I(0) uncertainty (real space) i0_real_error9.5190e+05
Rg (reciprocal space) rg_reciprocal27.39
I(0) (reciprocal space) i0_reciprocal67080000.0000
Solution quality estimate total_estimate0.9041
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.313
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17950000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)