6kbe

Structure of Deubiquitinase

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

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

Ubiquitin thioesterase

Oryza sativa subsp. japonica

UniProt B9G207

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 74–324 Not recorded Polyubiquitin-C × 1 (P0CG48) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;291 K;0.2 M Sodium chloride, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350 Resolution 2.34 Å R-free 0.256

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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B9G207_ORYSJ
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 3–253; UniProt 74–324

Polyubiquitin-C

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 G; UniProt 1–152 Non-standard monomer:Yes (specific site not provided by mmCIF) Ubiquitin thioesterase × 1 (B9G207) X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;291 K;0.2 M Sodium chloride, 0.1 M BIS-TRIS pH 5.5, 25% w/v Polyethylene glycol 3,350 Resolution 2.34 Å R-free 0.256

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 G; PDBConstruct 1–152; UniProt 1–152

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 6kbe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6kbe
Deposition date deposition_date2019-06-24
Structure title titleStructure of Deubiquitinase
Keywords keywordsIn complex with M1 type diUb, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.52
Radius of gyration Rg (electron density) rg_electron21.48
Forward intensity I(0) i032030400.00
Molecular weight molecular_weight44282.0 kDa
Excluded volume excluded_volume55774 ų
Envelope volume envelope_volume64631 ų
Hydration-shell volume shell_volume24846 ų
Envelope diameter envelope_diameter74.2
Shell Rg shell_rg28.70
Envelope Rg envelope_rg21.77
Shape Rg shape_rg21.46
Total Rg total_rg22.44
Total atoms total_atoms3120
Residues n_residues388
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_real22.43
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real3.2030e+07
I(0) uncertainty (real space) i0_real_error4.2060e+05
Rg (reciprocal space) rg_reciprocal22.45
I(0) (reciprocal space) i0_reciprocal32030000.0000
Solution quality estimate total_estimate0.8948
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.384
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7880000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6kbeb_
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
Domain ID domain_idd6kbeg1
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_idd6kbeg2
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 (2 domains)

Domain ID domain_id6kbeB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily60 — Peptidase C65 Otubain, subdomain 1
Domain ID domain_id6kbeB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1300 — 3 helical TM bundles of succinate and fumarate reductases
Homologous superfamily homologous superfamily20 — Peptidase C65 Otubain, subdomain 2

8. Citations (1)

9. Files and Curves (10)