2prk

SYNCHROTRON X-RAY DATA COLLECTION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 54.1 Å Quality: GOOD

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

PROTEINASE K

Engyodontium album

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 CA CALCIUM ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.50 Å

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_TRIAL
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 2prk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2prk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2prk
Deposition date deposition_date1987-11-30
Structure title titleSYNCHROTRON X-RAY DATA COLLECTION AND RESTRAINED LEAST-SQUARES REFINEMENT OF THE CRYSTAL STRUCTURE OF PROTEINASE K AT 1.5 ANGSTROMS RESOLUTION
Keywords keywordsSERINE PROTEINASE; SERINE PROTEINASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.88
Radius of gyration Rg (electron density) rg_electron16.78
Forward intensity I(0) i016077400.00
Molecular weight molecular_weight28800.0 kDa
Excluded volume excluded_volume35301 ų
Envelope volume envelope_volume38500 ų
Hydration-shell volume shell_volume18609 ų
Envelope diameter envelope_diameter56.0
Shell Rg shell_rg23.57
Envelope Rg envelope_rg17.04
Shape Rg shape_rg16.80
Total Rg total_rg17.62
Total atoms total_atoms2019
Residues n_residues279
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 dmax54.1
Rg (real space) rg_real17.70
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.6080e+07
I(0) uncertainty (real space) i0_real_error1.8160e+05
Rg (reciprocal space) rg_reciprocal17.73
I(0) (reciprocal space) i0_reciprocal16080000.0000
Solution quality estimate total_estimate0.8206
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.036
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4402000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2prka_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.41 — Subtilisin-like
Superfamily Superfamily superfamilyc.41.1 — Subtilisin-like
Family Family familyc.41.1.1 — Subtilases

CATH v4.4 (1 domains)

Domain ID domain_id2prkA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily200 — Peptidase S8/S53 domain

8. Citations (5)

9. Files and Curves (10)