8sog

Proteinase K Multiconformer Model at 313K

Method: X-RAY DIFFRACTION Dmax: 54.4 Å Quality: GOOD

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

Proteinase K

OrganismNot specified

UniProt P06873

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 106–384 Not recorded SO4 SULFATE ION × 3 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;Proteinase K was dissolved at pH 7.5 to 30 mg/mL in a 50 mM TRIS buffer. The protein was crystallized using a hanging drop setup on a 24 well VDX plate with sealant and 22 mm thick siliconized circle cover slides by mixing equal amounts of protein solution with 1.2 M ammonium sulfate. Resolution 1.13 Å R-free 0.151

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.

256 other PDB entries and 256 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRTK_PARAQ
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–279; UniProt 106–384

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 8sog

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sog
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8sog
Deposition date deposition_date2023-04-28
Structure title titleProteinase K Multiconformer Model at 313K
Keywords keywordsserine hydrolase, subtilisin-like, metal ion binding, a/b three-layered sandwiches, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.98
Radius of gyration Rg (electron density) rg_electron16.72
Forward intensity I(0) i013444100.00
Molecular weight molecular_weight25101.0 kDa
Excluded volume excluded_volume30413 ų
Envelope volume envelope_volume36674 ų
Hydration-shell volume shell_volume17988 ų
Envelope diameter envelope_diameter53.7
Shell Rg shell_rg23.17
Envelope Rg envelope_rg16.86
Shape Rg shape_rg16.73
Total Rg total_rg17.65
Total atoms total_atoms3397
Residues n_residues241
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 dmax54.4
Rg (real space) rg_real17.80
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.3440e+07
I(0) uncertainty (real space) i0_real_error1.4990e+05
Rg (reciprocal space) rg_reciprocal17.83
I(0) (reciprocal space) i0_reciprocal13440000.0000
Solution quality estimate total_estimate0.8989
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.024
Kurtosis Kurtosis kurtosis-0.486
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3045000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)