6jlq

Crystal structure of human USP46-WDR48-WDR20 complex

Method: X-RAY DIFFRACTION Dmax: 129.3 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 46

Homo sapiens

UniProt P62068

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 24–366 Not recorded WD repeat-containing protein 48 × 1 (Q8TAF3) WD repeat-containing protein 20,highly similar to WD repeat protein 20,WD repeat-containing protein 20 × 1 (Q8TBZ3,B3KQX8,L8I535) ZN ZINC ION × 1 GOL GLYCEROL × 8 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;1.0M Sodium phosphate monobasic monohydrate, Potassium phosphate dibasic, pH 7.2 Resolution 3.10 Å R-free 0.272

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBP46_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–344; UniProt 24–366

WD repeat-containing protein 48

Homo sapiens

UniProt Q8TAF3

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–580 Not recorded Ubiquitin carboxyl-terminal hydrolase 46 × 1 (P62068) WD repeat-containing protein 20,highly similar to WD repeat protein 20,WD repeat-containing protein 20 × 1 (Q8TBZ3,B3KQX8,L8I535) ZN ZINC ION × 1 GOL GLYCEROL × 8 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;1.0M Sodium phosphate monobasic monohydrate, Potassium phosphate dibasic, pH 7.2 Resolution 3.10 Å R-free 0.272

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.

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

View Construct and Data Evidence
UniProt name WDR48_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 41–620; UniProt 1–580

WD repeat-containing protein 20,highly similar to WD repeat protein 20,WD repeat-containing protein 20

Bos mutus

UniProt B3KQX8

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 106–137 Fragment:UNP residues 1-318,UNP residues 106-137,UNP residues 535-595 Ubiquitin carboxyl-terminal hydrolase 46 × 1 (P62068) WD repeat-containing protein 48 × 1 (Q8TAF3) ZN ZINC ION × 1 GOL GLYCEROL × 8 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;1.0M Sodium phosphate monobasic monohydrate, Potassium phosphate dibasic, pH 7.2 Resolution 3.10 Å R-free 0.272

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name B3KQX8_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 332–363; UniProt 106–137

WD repeat-containing protein 20,highly similar to WD repeat protein 20,WD repeat-containing protein 20

Bos mutus

UniProt L8I535

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 535–595 Fragment:UNP residues 1-318,UNP residues 106-137,UNP residues 535-595 Ubiquitin carboxyl-terminal hydrolase 46 × 1 (P62068) WD repeat-containing protein 48 × 1 (Q8TAF3) ZN ZINC ION × 1 GOL GLYCEROL × 8 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;1.0M Sodium phosphate monobasic monohydrate, Potassium phosphate dibasic, pH 7.2 Resolution 3.10 Å R-free 0.272

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name L8I535_9CETA
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 384–444; UniProt 535–595

WD repeat-containing protein 20,highly similar to WD repeat protein 20,WD repeat-containing protein 20

Bos mutus

UniProt Q8TBZ3

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–318 Fragment:UNP residues 1-318,UNP residues 106-137,UNP residues 535-595 Ubiquitin carboxyl-terminal hydrolase 46 × 1 (P62068) WD repeat-containing protein 48 × 1 (Q8TAF3) ZN ZINC ION × 1 GOL GLYCEROL × 8 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;1.0M Sodium phosphate monobasic monohydrate, Potassium phosphate dibasic, pH 7.2 Resolution 3.10 Å R-free 0.272

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WDR20_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 9–326; UniProt 1–318

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 6jlq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6jlq
Deposition date deposition_date2019-03-06
Structure title titleCrystal structure of human USP46-WDR48-WDR20 complex
Keywords keywordsDeubiquitinase, DUB, HYDROLASE, USP46; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.25
Radius of gyration Rg (electron density) rg_electron36.93
Forward intensity I(0) i0272473000.00
Molecular weight molecular_weight132640.0 kDa
Excluded volume excluded_volume165360 ų
Envelope volume envelope_volume219150 ų
Hydration-shell volume shell_volume49328 ų
Envelope diameter envelope_diameter138.0
Shell Rg shell_rg43.12
Envelope Rg envelope_rg36.80
Shape Rg shape_rg36.97
Total Rg total_rg37.18
Total atoms total_atoms9327
Residues n_residues1205
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 dmax129.3
Rg (real space) rg_real37.31
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real2.7250e+08
I(0) uncertainty (real space) i0_real_error4.2640e+06
Rg (reciprocal space) rg_reciprocal37.28
I(0) (reciprocal space) i0_reciprocal272500000.0000
Solution quality estimate total_estimate0.8745
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.9
Skewness Skewness skewness0.346
Kurtosis Kurtosis kurtosis-0.436
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha116200000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6jlqa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.3 — Cysteine proteinases
Superfamily Superfamily superfamilyd.3.1 — Cysteine proteinases
Family Family familyd.3.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id6jlqC00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)