6dgf

Ubiquitin Variant bound to USP2

Method: X-RAY DIFFRACTION Dmax: 70.5 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 2

Homo sapiens

UniProt O75604

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 250–605 Not recorded Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;0.1 M MES buffer pH 6, 12% (w/v) PEG3350, 0.2M sodium sulfate Resolution 2.34 Å R-free 0.224

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 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 15–370; UniProt 250–605

Polyubiquitin-B

Homo sapiens

UniProt P0CG47

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 153–226 Mutation:Q2C, K6C, K11R, T12C Ubiquitin carboxyl-terminal hydrolase 2 × 1 (O75604) ZN ZINC ION × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;0.1 M MES buffer pH 6, 12% (w/v) PEG3350, 0.2M sodium sulfate Resolution 2.34 Å R-free 0.224

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 20–93; UniProt 153–226

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 6dgf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6dgf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6dgf
Deposition date deposition_date2018-05-17
Structure title titleUbiquitin Variant bound to USP2
Keywords keywordsUbiquitin, Deubiquitinase, Ubiquitin Variant, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.40
Radius of gyration Rg (electron density) rg_electron20.86
Forward intensity I(0) i036549800.00
Molecular weight molecular_weight45423.0 kDa
Excluded volume excluded_volume56233 ų
Envelope volume envelope_volume65683 ų
Hydration-shell volume shell_volume25618 ų
Envelope diameter envelope_diameter72.8
Shell Rg shell_rg28.29
Envelope Rg envelope_rg21.14
Shape Rg shape_rg20.79
Total Rg total_rg21.94
Total atoms total_atoms3183
Residues n_residues406
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 dmax70.5
Rg (real space) rg_real22.28
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real3.6550e+07
I(0) uncertainty (real space) i0_real_error4.8770e+05
Rg (reciprocal space) rg_reciprocal22.31
I(0) (reciprocal space) i0_reciprocal36550000.0000
Solution quality estimate total_estimate0.8939
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.190
Kurtosis Kurtosis kurtosis-0.360
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6980000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6dgfa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.3 — Cysteine proteinases
Superfamily Superfamily superfamilyd.3.1 — Cysteine proteinases
Family Family familyd.3.1.9 — Ubiquitin carboxyl-terminal hydrolase, UCH
Domain ID domain_idd6dgfb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd6dgfb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id6dgfA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily10 — Cysteine proteinases

8. Citations (1)

9. Files and Curves (10)