3znz

Crystal structure of OTULIN OTU domain (C129A) in complex with Met1- di ubiquitin

Method: X-RAY DIFFRACTION Dmax: 73.4 Å Quality: GOOD

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

PROTEIN FAM105B

HOMO SAPIENS

UniProt Q96BN8

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 80–352 Fragment:OTU DOMAIN, RESIDUES 80-352 Mutation:YES POLYUBIQUITIN-C × 1 (F5H265) SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;100 MM BIS-TRIS, 2M (NH4)2SO4, PH 6.5 Resolution 1.90 Å R-free 0.222

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.

11 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F105B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–275; UniProt 80–352

POLYUBIQUITIN-C

HOMO SAPIENS

UniProt F5H265

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 1–149 Not recorded PROTEIN FAM105B × 1 (Q96BN8) SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;100 MM BIS-TRIS, 2M (NH4)2SO4, PH 6.5 Resolution 1.90 Å R-free 0.222

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 F5H265_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–149; UniProt 1–149

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 3znz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3znz
Deposition date deposition_date2013-02-18
Structure title titleCrystal structure of OTULIN OTU domain (C129A) in complex with Met1- di ubiquitin
Keywords keywordsHYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.79
Radius of gyration Rg (electron density) rg_electron21.72
Forward intensity I(0) i038437900.00
Molecular weight molecular_weight47483.0 kDa
Excluded volume excluded_volume59345 ų
Envelope volume envelope_volume68859 ų
Hydration-shell volume shell_volume26013 ų
Envelope diameter envelope_diameter76.1
Shell Rg shell_rg28.87
Envelope Rg envelope_rg21.97
Shape Rg shape_rg21.70
Total Rg total_rg22.65
Total atoms total_atoms3329
Residues n_residues412
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 dmax73.4
Rg (real space) rg_real22.67
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real3.8440e+07
I(0) uncertainty (real space) i0_real_error4.0580e+05
Rg (reciprocal space) rg_reciprocal22.70
I(0) (reciprocal space) i0_reciprocal38440000.0000
Solution quality estimate total_estimate0.8938
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.171
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8960000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3znzb1
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_idd3znzb2
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_id3znzB01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id3znzB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)