7zjv

Structure of human USPL1 in covalent complex with DeltaN-SUMO2/3-PA probe

Method: X-RAY DIFFRACTION Dmax: 73.8 Å Quality: GOOD

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

SUMO-specific isopeptidase USPL1

Homo sapiens

UniProt Q5W0Q7

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 A; UniProt 218–502 Not recorded Small ubiquitin-related modifier 2 × 1 (P61956) ZN ZINC ION × 1 AYE prop-2-en-1-amine × 1 CL CHLORIDE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.9;293 K;100 mM CHES pH 8.9, 34% PEG600 Resolution 2.40 Å R-free 0.258

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name USPL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–287; UniProt 218–502

Small ubiquitin-related modifier 2

Homo sapiens

UniProt P61956

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 18–92 Not recorded SUMO-specific isopeptidase USPL1 × 1 (Q5W0Q7) ZN ZINC ION × 1 AYE prop-2-en-1-amine × 1 CL CHLORIDE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.9;293 K;100 mM CHES pH 8.9, 34% PEG600 Resolution 2.40 Å R-free 0.258

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.

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

View Construct and Data Evidence
UniProt name SUMO2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–76; UniProt 18–92

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 7zjv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7zjv
Deposition date deposition_date2022-04-12
Structure title titleStructure of human USPL1 in covalent complex with DeltaN-SUMO2/3-PA probe
Keywords keywordsUSP, SUMO, Ubiquitin, probe, ubiquitin-like modifier, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.76
Radius of gyration Rg (electron density) rg_electron20.33
Forward intensity I(0) i025146400.00
Molecular weight molecular_weight37505.0 kDa
Excluded volume excluded_volume46433 ų
Envelope volume envelope_volume54735 ų
Hydration-shell volume shell_volume22399 ų
Envelope diameter envelope_diameter76.2
Shell Rg shell_rg27.13
Envelope Rg envelope_rg20.66
Shape Rg shape_rg20.29
Total Rg total_rg21.33
Total atoms total_atoms2631
Residues n_residues336
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 dmax73.8
Rg (real space) rg_real21.68
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real2.5150e+07
I(0) uncertainty (real space) i0_real_error3.5290e+05
Rg (reciprocal space) rg_reciprocal21.70
I(0) (reciprocal space) i0_reciprocal25150000.0000
Solution quality estimate total_estimate0.8759
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.5
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.281
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4920000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.798; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)