5gvi

Zebrafish USP30 in complex with Lys6-linked diubiquitin

Method: X-RAY DIFFRACTION Dmax: 89.0 Å Quality: GOOD

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

Ubiquitin carboxyl-terminal hydrolase 30

Danio rerio

UniProt A0A0R4ILB8

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 61–501 Fragment:UNP residues 61-501 Mutation:C73A, D127V ubiquitin × 1 (P62983) ubiquitin × 1 (P62983) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;90 mM Tris-HCl, 180 mM ammonium acetate, 23% PEG3350, 10 mM TCEP Resolution 1.87 Å R-free 0.206

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 A0A0R4ILB8_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–444; UniProt 61–501

ubiquitin

Mus musculus

UniProt P62983

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–76 Chain C; UniProt 1–72 Mutation:K6R Ubiquitin carboxyl-terminal hydrolase 30 × 1 (A0A0R4ILB8) ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;90 mM Tris-HCl, 180 mM ammonium acetate, 23% PEG3350, 10 mM TCEP Resolution 1.87 Å R-free 0.206

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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RS27A_MOUSE
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–76; UniProt 1–76 Author chain C; PDBConstruct 1–72; UniProt 1–72

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 5gvi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5gvi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5gvi
Deposition date deposition_date2016-09-05
Structure title titleZebrafish USP30 in complex with Lys6-linked diubiquitin
Keywords keywordsComplex, mitophagy, Hydrolase-SIGNALING PROTEIN complex; Hydrolase/SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.27
Radius of gyration Rg (electron density) rg_electron24.16
Forward intensity I(0) i049430100.00
Molecular weight molecular_weight53842.0 kDa
Excluded volume excluded_volume67117 ų
Envelope volume envelope_volume81275 ų
Hydration-shell volume shell_volume28424 ų
Envelope diameter envelope_diameter95.0
Shell Rg shell_rg31.08
Envelope Rg envelope_rg24.75
Shape Rg shape_rg24.09
Total Rg total_rg25.11
Total atoms total_atoms3781
Residues n_residues474
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 dmax89.0
Rg (real space) rg_real25.31
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real4.9430e+07
I(0) uncertainty (real space) i0_real_error6.5350e+05
Rg (reciprocal space) rg_reciprocal25.30
I(0) (reciprocal space) i0_reciprocal49430000.0000
Solution quality estimate total_estimate0.8469
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.500
Kurtosis Kurtosis kurtosis0.084
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9846000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.696; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5gvib_
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_idd5gvic_
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_id5gviA01
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)