3wxe

Crystal structure of CYLD USP domain (C596S) in complex with Met1-linked diubiquitin

Method: X-RAY DIFFRACTION Dmax: 72.0 Å Quality: EXCELLENT

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

Uncharacterized protein

Danio rerio

UniProt E7FEV5

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 578–780 Chain A; UniProt 850–951 Fragment:USP domain, UNP residues 578-780, Linker, 850-951 Mutation:C596S, B-box deletion Ubiquitin × 1 (P0CG48) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;50mM Tris-HCl buffer, 9% PEG4000, 100mM magnesium chloride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.247

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 E7FEV5_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–206; UniProt 578–780 Author chain A; PDBConstruct 211–312; UniProt 850–951

Ubiquitin

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 B; UniProt 1–148 Not recorded Uncharacterized protein × 1 (E7FEV5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;50mM Tris-HCl buffer, 9% PEG4000, 100mM magnesium chloride, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.50 Å R-free 0.247

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 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–148; UniProt 1–148

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 3wxe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3wxe
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3wxe
Deposition date deposition_date2014-07-30
Structure title titleCrystal structure of CYLD USP domain (C596S) in complex with Met1-linked diubiquitin
Keywords keywordsubiquitin protease, HYDROLASE-PROTEIN BINDING complex; HYDROLASE/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.45
Radius of gyration Rg (electron density) rg_electron22.21
Forward intensity I(0) i042552000.00
Molecular weight molecular_weight51512.0 kDa
Excluded volume excluded_volume65024 ų
Envelope volume envelope_volume76444 ų
Hydration-shell volume shell_volume27930 ų
Envelope diameter envelope_diameter74.4
Shell Rg shell_rg30.04
Envelope Rg envelope_rg22.52
Shape Rg shape_rg22.20
Total Rg total_rg23.20
Total atoms total_atoms3617
Residues n_residues449
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 dmax72.0
Rg (real space) rg_real23.30
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real4.2550e+07
I(0) uncertainty (real space) i0_real_error4.5640e+05
Rg (reciprocal space) rg_reciprocal23.34
I(0) (reciprocal space) i0_reciprocal42550000.0000
Solution quality estimate total_estimate0.9029
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.164
Kurtosis Kurtosis kurtosis-0.431
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11000000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3wxeb1
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_idd3wxeb2
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

CATH v4.4 (1 domains)

Domain ID domain_id3wxeA00
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)