4cha

STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 73.4 Å Quality: GOOD

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

ALPHA-CHYMOTRYPSIN 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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) 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 No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.68 Å

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

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 4cha

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cha
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cha
Deposition date deposition_date1984-11-26
Structure title titleSTRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION
Keywords keywordsHYDROLASE (SERINE PROTEINASE); HYDROLASE (SERINE PROTEINASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.02
Radius of gyration Rg (electron density) rg_electron22.29
Forward intensity I(0) i042810500.00
Molecular weight molecular_weight50032.0 kDa
Excluded volume excluded_volume62424 ų
Envelope volume envelope_volume73358 ų
Hydration-shell volume shell_volume26969 ų
Envelope diameter envelope_diameter75.2
Shell Rg shell_rg29.61
Envelope Rg envelope_rg22.46
Shape Rg shape_rg22.27
Total Rg total_rg23.18
Total atoms total_atoms3506
Residues n_residues477
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 dmax73.4
Rg (real space) rg_real22.96
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real4.2810e+07
I(0) uncertainty (real space) i0_real_error5.7240e+05
Rg (reciprocal space) rg_reciprocal22.98
I(0) (reciprocal space) i0_reciprocal42810000.0000
Solution quality estimate total_estimate0.8938
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26140000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.873; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4cha.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
Domain ID domain_idd4cha.2
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 (4 domains)

Domain ID domain_id4chaB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4chaC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4chaF00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id4chaG00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (15)

9. Files and Curves (10)