Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3I29

Crystal structure of a binary complex between an mutant trypsin inhibitor with bovine trypsin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
A0097180cellular_componentserine protease inhibitor complex
A0097655molecular_functionserpin family protein binding
B0004866molecular_functionendopeptidase inhibitor activity
B0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 991
ChainResidue
AGLU70
AASN72
AVAL75
AVAL76
AGLU80

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
AASP189-VAL200

site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LvDAEGNlVeNGgtYyL
ChainResidueDetails
BLEU4-LEU20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond for chymotrypsin
ChainResidueDetails
BARG65
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
AGLU70
AASN72
AVAL75
AGLU80
AASP189
AGLN192
ASER195

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon