Structure analysis

CRYSTAL STRUCTURE OF GAMMA CHYMOTRYPSIN WITH N-ACETYL-LEUCIL-PHENYLALANINE ALDEHYDE BOUND AT THE ACTIVE SITE

X-ray diffraction
1.5Å resolution
Source organism: Bos taurus
Assemblies composition:
hetero trimer (preferred)
hetero hexamer
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 9911.71 Å2
Buried surface area: 7907.67 Å2
Dissociation area: 680.69 Å2
Dissociation energy (ΔGdiss): 8.65 kcal/mol
Dissociation entropy (TΔSdiss): 7.2 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133405
Assembly 2
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Multimeric state: hetero hexamer
Accessible surface area: 17607.4 Å2
Buried surface area: 18027.85 Å2
Dissociation area: 1,359.33 Å2
Dissociation energy (ΔGdiss): 17.18 kcal/mol
Dissociation entropy (TΔSdiss): 14.46 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-133435
Assembly 3
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Multimeric state: hetero hexamer
Accessible surface area: 19103.78 Å2
Buried surface area: 16531.47 Å2
Dissociation area: 584.23 Å2
Dissociation energy (ΔGdiss): 2.09 kcal/mol
Dissociation entropy (TΔSdiss): 14.3 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-133435

Macromolecules

Chain: A
Length: 10 amino acids
Theoretical weight: 996 Da
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 1-10; Coverage: 4%)
SCOP: Eukaryotic proteases
PDBe-KB: UniProt Coverage View: P00766  
11012345678910
 
510CGVPAIQPVL
UniProt
P00766
Chains
Domains
Flexibility predictions
Interaction interfaces

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PDBe-KB: UniProt Coverage View: P00766  
1131102030405060708090100110120130
 
50100
UniProt
P00766
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

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Chain: C
Length: 97 amino acids
Theoretical weight: 10.07 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00766 (Residues: 149-245; Coverage: 40%)
Pfam: Trypsin
InterPro:
CATH: Trypsin-like serine proteases
SCOP: Eukaryotic proteases
PDBe-KB: UniProt Coverage View: P00766  
197102030405060708090
 
50
UniProt
P00766
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites
Interaction interfaces
Sequence conservation

Search similar proteins