5r46

Crystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, room temperature

Method: X-RAY DIFFRACTION Dmax: 53.9 Å Quality: GOOD

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

gamma-chymotrypsin

OrganismNot specified

UniProt P00766

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–13 Chain B; UniProt 16–146 Chain C; UniProt 149–245 Not recorded peptide SWPW × 1 peptide TPGVY × 1 IOD IODIDE ION × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;297 K;45% saturated ammonium sulfate, 0.75% saturated cetyltrimethylammonium bromide, 100 mM sodium iodide; sodium malonate Resolution 1.05 Å R-free 0.122

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.

91 other PDB entries and 177 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CTRA_BOVIN
Isoform
PDB entities 1, 2, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–13; UniProt 1–13 Author chain B; PDBConstruct 1–131; UniProt 16–146 Author chain C; PDBConstruct 1–97; UniProt 149–245

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 5r46

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5r46
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5r46
Deposition date deposition_date2020-02-18
Structure title titleCrystal Structure of deuterated gamma-Chymotrypsin at pH 5.6, room temperature
Keywords keywordsserine protease, hydrolase-peptide complex, Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.54
Radius of gyration Rg (electron density) rg_electron16.33
Forward intensity I(0) i012358900.00
Molecular weight molecular_weight25664.0 kDa
Excluded volume excluded_volume31828 ų
Envelope volume envelope_volume35625 ų
Hydration-shell volume shell_volume17708 ų
Envelope diameter envelope_diameter56.4
Shell Rg shell_rg23.04
Envelope Rg envelope_rg16.67
Shape Rg shape_rg16.28
Total Rg total_rg17.49
Total atoms total_atoms1789
Residues n_residues240
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 dmax53.9
Rg (real space) rg_real17.39
Rg uncertainty (real space) rg_real_error0.20
I(0) (real space) i0_real1.2360e+07
I(0) uncertainty (real space) i0_real_error1.3190e+05
Rg (reciprocal space) rg_reciprocal17.41
I(0) (reciprocal space) i0_reciprocal12360000.0000
Solution quality estimate total_estimate0.8203
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.068
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3829000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)