Function and Biology Details
Reaction catalysed:
Preferential cleavage: -Asp-|- >> -Asn-|- > -Met-|-, -Ser-|-.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Proteinase inhibitor I11, ecotin
- Peptidase S1A, chymotrypsin family
- Serine proteases, trypsin domain
- Ecotin superfamily
- Peptidase S1, PA clan, chymotrypsin-like fold
- Ecotin, C-terminal
- Serine proteases, trypsin family, serine active site
- Serine proteases, trypsin family, histidine active site
1 more domain
Structure domains:
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
Assembly name:
Granzyme B and Ecotin (preferred)
PDBe Complex ID:
PDB-CPX-148347 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Granzyme B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 25.23 KDa
Source organism: Rattus norvegicus
Expression system: Komagataella pastoris
UniProt:
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Length: 228 amino acids
Theoretical weight: 25.23 KDa
Source organism: Rattus norvegicus
Expression system: Komagataella pastoris
UniProt:
- Canonical:
P18291 (Residues: 21-248; Coverage: 99%)
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases
Ecotin
Ecotin
Molecule details ›
Chains: D, F
Length: 58 amino acids
Theoretical weight: 6.65 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Ecotin
Structure domains: Ecotin, trypsin inhibitor
Length: 58 amino acids
Theoretical weight: 6.65 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P23827 (Residues: 105-162; Coverage: 41%)
Sequence domains: Ecotin
Structure domains: Ecotin, trypsin inhibitor
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL9-1
Spacegroup:
P21
Expression systems:
- Komagataella pastoris
- Escherichia coli
