7qir

CRYSTAL STRUCTURE OF THE P1 monofluorethylglycine(MfeGly) BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX

Method: X-RAY DIFFRACTION Dmax: 98.0 Å Quality: REASONABLE

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

Chymotrypsin A chain A

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–13 Chain B; UniProt 16–146 Chain C; UniProt 149–245 Chain E; UniProt 1–13 Chain F; UniProt 16–146 Chain G; UniProt 149–245 Not recorded Pancreatic trypsin inhibitor × 2 (P00974) GOL GLYCEROL × 28 SO4 SULFATE ION × 17 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;1.8 M ammonium sulfate and 0.1 M MES/NaOH (pH 6.5) Resolution 1.90 Å R-free 0.189

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 E; PDBConstruct 1–13; UniProt 1–13 Author chain B; PDBConstruct 1–131; UniProt 16–146 Author chain F; PDBConstruct 1–131; UniProt 16–146 Author chain C; PDBConstruct 1–97; UniProt 149–245 Author chain G; PDBConstruct 1–97; UniProt 149–245

Pancreatic trypsin inhibitor

OrganismNot specified

UniProt P00974

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 36–93 Chain H; UniProt 36–93 Non-standard monomer:Yes (specific site not provided by mmCIF) Chymotrypsin A chain A × 2 (P00766) Chymotrypsin A chain B × 2 (P00766) Chymotrypsin A chain C × 2 (P00766) GOL GLYCEROL × 28 SO4 SULFATE ION × 17 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;1.8 M ammonium sulfate and 0.1 M MES/NaOH (pH 6.5) Resolution 1.90 Å R-free 0.189

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.

123 other PDB entries and 265 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BPT1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–58; UniProt 36–93 Author chain H; PDBConstruct 1–58; UniProt 36–93

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 7qir

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7qir
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7qir
Deposition date deposition_date2021-12-15
Structure title titleCRYSTAL STRUCTURE OF THE P1 monofluorethylglycine(MfeGly) BPTI MUTANT- BOVINE CHYMOTRYPSIN COMPLEX
Keywords keywords;CHYMOTRYPSIN, SERINE PROTEINASE, BOVINE PANCREATIC TRYPSIN INHIBITOR, BPTI, PROTEIN-PROTEIN INTERACTION, S1 POCKET, PRIMARY SPECIFICITY, HYDROLASE-HYDROLASE INHIBITOR COMPLEX, HYDROLASE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.19
Radius of gyration Rg (electron density) rg_electron30.21
Forward intensity I(0) i079008400.00
Molecular weight molecular_weight66967.0 kDa
Excluded volume excluded_volume82515 ų
Envelope volume envelope_volume101370 ų
Hydration-shell volume shell_volume29311 ų
Envelope diameter envelope_diameter103.9
Shell Rg shell_rg35.74
Envelope Rg envelope_rg30.05
Shape Rg shape_rg30.18
Total Rg total_rg30.77
Total atoms total_atoms4651
Residues n_residues593
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 dmax98.0
Rg (real space) rg_real30.42
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real7.9010e+07
I(0) uncertainty (real space) i0_real_error1.2800e+06
Rg (reciprocal space) rg_reciprocal30.33
I(0) (reciprocal space) i0_reciprocal79000000.0000
Solution quality estimate total_estimate0.6374
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.617
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27370000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.778; Smooth: 0.735

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)