1ab9

CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN

Method: X-RAY DIFFRACTION Dmax: 56.5 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 × 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 PENTAPEPTIDE (TPGVY) × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;ALPHA-CHYMOTRYPSIN WAS DISSOLVED IN POTASSIUM BORATE (PH8.6) AND WAS INCUBATED AT 310K FOR 6 HOURS. SOLID AMMONIUM SULFATE WAS ADDED TO THE SOLUTION, AND THE PRECIPITATE FORMED WAS RECOVERED AND RE-DISSOLVED WITH WATER. CRYSTALLIZATION WAS DONE WITH A SITTING-DROP VAPOR-DIFFUSION PROCEDURE, IN WHICH PROTEIN SOLUTION (15MG/ML) CONTAINING 10MM CACODYLATE, 0.75% SATURATED ACETYLTRIMETHYL AMMONIUM AND 45% SATURATED AMMONIUM SULFATE WAS EQUILIBRATED AGAINST 65% SATURATED AMMONIUM SULFATE AT 293K., pH 5.6, vapor diffusion - sitting drop Resolution 1.60 Å R-free 0.190
2 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 Not recorded PENTAPEPTIDE (TPGVY) × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;ALPHA-CHYMOTRYPSIN WAS DISSOLVED IN POTASSIUM BORATE (PH8.6) AND WAS INCUBATED AT 310K FOR 6 HOURS. SOLID AMMONIUM SULFATE WAS ADDED TO THE SOLUTION, AND THE PRECIPITATE FORMED WAS RECOVERED AND RE-DISSOLVED WITH WATER. CRYSTALLIZATION WAS DONE WITH A SITTING-DROP VAPOR-DIFFUSION PROCEDURE, IN WHICH PROTEIN SOLUTION (15MG/ML) CONTAINING 10MM CACODYLATE, 0.75% SATURATED ACETYLTRIMETHYL AMMONIUM AND 45% SATURATED AMMONIUM SULFATE WAS EQUILIBRATED AGAINST 65% SATURATED AMMONIUM SULFATE AT 293K., pH 5.6, vapor diffusion - sitting drop Resolution 1.60 Å R-free 0.190
3 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 Not recorded PENTAPEPTIDE (TPGVY) × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;ALPHA-CHYMOTRYPSIN WAS DISSOLVED IN POTASSIUM BORATE (PH8.6) AND WAS INCUBATED AT 310K FOR 6 HOURS. SOLID AMMONIUM SULFATE WAS ADDED TO THE SOLUTION, AND THE PRECIPITATE FORMED WAS RECOVERED AND RE-DISSOLVED WITH WATER. CRYSTALLIZATION WAS DONE WITH A SITTING-DROP VAPOR-DIFFUSION PROCEDURE, IN WHICH PROTEIN SOLUTION (15MG/ML) CONTAINING 10MM CACODYLATE, 0.75% SATURATED ACETYLTRIMETHYL AMMONIUM AND 45% SATURATED AMMONIUM SULFATE WAS EQUILIBRATED AGAINST 65% SATURATED AMMONIUM SULFATE AT 293K., pH 5.6, vapor diffusion - sitting drop Resolution 1.60 Å R-free 0.190

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 175 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 1ab9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ab9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ab9
Deposition date deposition_date1997-02-05
Structure title titleCRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN
Keywords keywords;HYDROLASE, SERINE PROTEASE, DIGESTION, PANCREAS, ZYMOGEN, COMPLEX (SERINE PROTEASE-PEPTIDE), COMPLEX (SERINE PROTEASE-PEPTIDE) complex ;; COMPLEX (SERINE PROTEASE/PEPTIDE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.55
Radius of gyration Rg (electron density) rg_electron16.35
Forward intensity I(0) i012053700.00
Molecular weight molecular_weight25516.0 kDa
Excluded volume excluded_volume31808 ų
Envelope volume envelope_volume35734 ų
Hydration-shell volume shell_volume17727 ų
Envelope diameter envelope_diameter55.3
Shell Rg shell_rg23.06
Envelope Rg envelope_rg16.71
Shape Rg shape_rg16.32
Total Rg total_rg17.50
Total atoms total_atoms1787
Residues n_residues242
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 dmax56.5
Rg (real space) rg_real17.40
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.2050e+07
I(0) uncertainty (real space) i0_real_error1.3560e+05
Rg (reciprocal space) rg_reciprocal17.42
I(0) (reciprocal space) i0_reciprocal12050000.0000
Solution quality estimate total_estimate0.8045
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.077
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4300000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.821; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1ab9.1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id1ab9B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1ab9C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (4)

9. Files and Curves (10)