9f6h

Crystal structure of bovine alpha-chymotrypsin in complex with the bicyclic peptide inhibitor MP5.4.3

Method: X-RAY DIFFRACTION Dmax: 55.6 Å Quality: GOOD

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–13 Chain B; UniProt 16–146 Chain C; UniProt 149–245 Not recorded Bicyclic peptide MP5.4.3 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;70% v/v MPD, 0.1 M HEPES, pH 7.5. Resolution 2.42 Å R-free 0.286

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 9f6h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f6h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f6h
Deposition date deposition_date2024-05-01
Structure title titleCrystal structure of bovine alpha-chymotrypsin in complex with the bicyclic peptide inhibitor MP5.4.3
Keywords keywordsSerine protease; Bicyclic peptide, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.85
Radius of gyration Rg (electron density) rg_electron16.68
Forward intensity I(0) i013175200.00
Molecular weight molecular_weight26692.0 kDa
Excluded volume excluded_volume33224 ų
Envelope volume envelope_volume38304 ų
Hydration-shell volume shell_volume18618 ų
Envelope diameter envelope_diameter56.4
Shell Rg shell_rg23.45
Envelope Rg envelope_rg16.91
Shape Rg shape_rg16.66
Total Rg total_rg17.77
Total atoms total_atoms1866
Residues n_residues255
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 dmax55.6
Rg (real space) rg_real17.68
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.3180e+07
I(0) uncertainty (real space) i0_real_error1.3520e+05
Rg (reciprocal space) rg_reciprocal17.70
I(0) (reciprocal space) i0_reciprocal13180000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.052
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5893000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)