9pda

Structure of Porcine Trypsin Crystals Grown From PEG and Complexed With Crystallization Additives IV

Method: X-RAY DIFFRACTION Dmax: 140.8 Å Quality: GOOD

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

Trypsin

Sus scrofa

UniProt P00761

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 1–231 Not recorded BEN BENZAMIDINE × 1 PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE × 3 PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE × 1 PEG DI(HYDROXYETHYL)ETHER × 8 CA CALCIUM ION × 1 MLI MALONATE ION × 1 PG4 TETRAETHYLENE GLYCOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;Sitting drop vapor diffusion in Cryschem plates with reservoirs of 30% PEG 3350 buffered at pH 6.5 with 0.1 M HEPES. Drops composed of 3 ul reservoir, 2 ul of additive mix (oxalic acid, malic acid, oxaloacetic acid, pyromellitic acid), and 3 ul of a 40 mg/ml protein stock Resolution 1.18 Å R-free 0.230
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–231 Not recorded BEN BENZAMIDINE × 3 PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE × 4 PEG DI(HYDROXYETHYL)ETHER × 18 CA CALCIUM ION × 1 MLI MALONATE ION × 1 PG4 TETRAETHYLENE GLYCOL × 3 PMA PYROMELLITIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;Sitting drop vapor diffusion in Cryschem plates with reservoirs of 30% PEG 3350 buffered at pH 6.5 with 0.1 M HEPES. Drops composed of 3 ul reservoir, 2 ul of additive mix (oxalic acid, malic acid, oxaloacetic acid, pyromellitic acid), and 3 ul of a 40 mg/ml protein stock Resolution 1.18 Å R-free 0.230
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–231 Not recorded BEN BENZAMIDINE × 3 PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE × 2 PEG DI(HYDROXYETHYL)ETHER × 15 CA CALCIUM ION × 1 MLI MALONATE ION × 1 PG4 TETRAETHYLENE GLYCOL × 5 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;Sitting drop vapor diffusion in Cryschem plates with reservoirs of 30% PEG 3350 buffered at pH 6.5 with 0.1 M HEPES. Drops composed of 3 ul reservoir, 2 ul of additive mix (oxalic acid, malic acid, oxaloacetic acid, pyromellitic acid), and 3 ul of a 40 mg/ml protein stock Resolution 1.18 Å R-free 0.230
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–231 Not recorded BEN BENZAMIDINE × 3 PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE × 3 PEG DI(HYDROXYETHYL)ETHER × 20 CA CALCIUM ION × 2 MLI MALONATE ION × 1 PG4 TETRAETHYLENE GLYCOL × 6 PMA PYROMELLITIC ACID × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;Sitting drop vapor diffusion in Cryschem plates with reservoirs of 30% PEG 3350 buffered at pH 6.5 with 0.1 M HEPES. Drops composed of 3 ul reservoir, 2 ul of additive mix (oxalic acid, malic acid, oxaloacetic acid, pyromellitic acid), and 3 ul of a 40 mg/ml protein stock Resolution 1.18 Å R-free 0.230

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.

44 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRYP_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–231; UniProt 1–231 Author chain B; PDBConstruct 1–231; UniProt 1–231 Author chain C; PDBConstruct 1–231; UniProt 1–231 Author chain D; PDBConstruct 1–231; UniProt 1–231

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 9pda

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9pda
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9pda
Deposition date deposition_date2025-06-30
Structure title titleStructure of Porcine Trypsin Crystals Grown From PEG and Complexed With Crystallization Additives IV
Keywords keywordsCrystallization, additives, PEG, Silver Bullets, ligands, solvent regions, refinement, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.60
Radius of gyration Rg (electron density) rg_electron41.76
Forward intensity I(0) i0182320000.00
Molecular weight molecular_weight109100.0 kDa
Excluded volume excluded_volume136480 ų
Envelope volume envelope_volume194340 ų
Hydration-shell volume shell_volume40481 ų
Envelope diameter envelope_diameter146.0
Shell Rg shell_rg44.50
Envelope Rg envelope_rg41.01
Shape Rg shape_rg41.76
Total Rg total_rg41.91
Total atoms total_atoms15256
Residues n_residues892
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 dmax140.8
Rg (real space) rg_real41.88
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real1.8230e+08
I(0) uncertainty (real space) i0_real_error3.3830e+06
Rg (reciprocal space) rg_reciprocal41.60
I(0) (reciprocal space) i0_reciprocal182300000.0000
Solution quality estimate total_estimate0.8142
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.694
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14270000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.737; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.704; Smooth: 0.667

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)