6hei

Structure of the catalytic domain of USP28 (insertion deleted) bound to Ubiquitin-PA

Method: X-RAY DIFFRACTION Dmax: 83.0 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 28,Ubiquitin carboxyl-terminal hydrolase 28

Homo sapiens

UniProt Q96RU2

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 149–399 Chain A; UniProt 580–703 Mutation:;residues 400-579 replaced by GSGSGS,residues 400-579 replaced by GSGSGS,residues 400-579 replaced by GSGSGS,residues 400-579 replaced by GSGSGS ; Polyubiquitin-B × 1 (P0CG47) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;291 K;22% (w/v) PEG 3350, 300 mM potassium sodium tartrate Resolution 1.64 Å R-free 0.214

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.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP28_HUMAN
Isoform Q96RU2-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–252; UniProt 149–399 Author chain A; PDBConstruct 259–382; UniProt 580–703

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 77–151 Mutation:residue 76 replaced with PA warhead Non-standard monomer:Yes (specific site not provided by mmCIF) Ubiquitin carboxyl-terminal hydrolase 28,Ubiquitin carboxyl-terminal hydrolase 28 × 1 (Q96RU2) EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;291 K;22% (w/v) PEG 3350, 300 mM potassium sodium tartrate Resolution 1.64 Å R-free 0.214

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 3–77; UniProt 77–151

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 6hei

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6hei
Deposition date deposition_date2018-08-20
Structure title titleStructure of the catalytic domain of USP28 (insertion deleted) bound to Ubiquitin-PA
Keywords keywordsUbiquitin, USP, Ubiquitin-specific protease, DUB, Deubiquitinase, protease, isopeptidase, USP28, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.69
Radius of gyration Rg (electron density) rg_electron22.25
Forward intensity I(0) i038692500.00
Molecular weight molecular_weight48170.0 kDa
Excluded volume excluded_volume60268 ų
Envelope volume envelope_volume72139 ų
Hydration-shell volume shell_volume26718 ų
Envelope diameter envelope_diameter85.9
Shell Rg shell_rg29.60
Envelope Rg envelope_rg22.68
Shape Rg shape_rg22.25
Total Rg total_rg23.13
Total atoms total_atoms3403
Residues n_residues422
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 dmax83.0
Rg (real space) rg_real23.60
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real3.8690e+07
I(0) uncertainty (real space) i0_real_error5.1280e+05
Rg (reciprocal space) rg_reciprocal23.62
I(0) (reciprocal space) i0_reciprocal38690000.0000
Solution quality estimate total_estimate0.7763
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.284
Kurtosis Kurtosis kurtosis-0.173
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8022000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.702; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6heib1
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_idd6heib2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6heib3
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_id6heiA01
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)