3znv

Crystal structure of the OTU domain of OTULIN at 1.3 Angstroms.

Method: X-RAY DIFFRACTION Dmax: 64.1 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 80–352 Fragment:OTU DOMAIN, RESIDUES 80-352 GOL GLYCEROL × 4 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;100 MM MES/IMIDAZOLE PH 6.5, 30 MM MGCL2, 30 MM CACL2, 10% PEG 4000, 20% GLYCEROL Resolution 1.30 Å R-free 0.154

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

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 3znv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3znv
Deposition date deposition_date2013-02-18
Structure title titleCrystal structure of the OTU domain of OTULIN at 1.3 Angstroms.
Keywords keywordsHYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.05
Radius of gyration Rg (electron density) rg_electron18.82
Forward intensity I(0) i016517800.00
Molecular weight molecular_weight31234.0 kDa
Excluded volume excluded_volume39338 ų
Envelope volume envelope_volume44926 ų
Hydration-shell volume shell_volume19923 ų
Envelope diameter envelope_diameter65.9
Shell Rg shell_rg25.24
Envelope Rg envelope_rg19.14
Shape Rg shape_rg18.77
Total Rg total_rg19.90
Total atoms total_atoms2194
Residues n_residues269
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 dmax64.1
Rg (real space) rg_real19.98
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.6520e+07
I(0) uncertainty (real space) i0_real_error2.0650e+05
Rg (reciprocal space) rg_reciprocal19.99
I(0) (reciprocal space) i0_reciprocal16520000.0000
Solution quality estimate total_estimate0.8943
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.242
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3025000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)