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3VEQ

A binary complex betwwen bovine pancreatic trypsin and a engineered mutant trypsin inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0007586biological_processdigestion
B0008236molecular_functionserine-type peptidase activity
B0046872molecular_functionmetal ion binding
B0097180cellular_componentserine protease inhibitor complex
B0097655molecular_functionserpin family protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 301
ChainResidue
BGLU67
BASN69
BVAL72
BGLU77

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
BVAL51-CYS56

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
BASP186-VAL197

site_idPS00283
Number of Residues17
DetailsSOYBEAN_KUNITZ Soybean trypsin inhibitor (Kunitz) protease inhibitors family signature. LvDAEGNlVeNGgtYyL
ChainResidueDetails
ALEU607-LEU623

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond for chymotrypsin
ChainResidueDetails
AARG668
BASP99
BSER192

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
BGLU67
BASN69
BVAL72
BGLU77
BASP186
BGLN189
BSER192

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PDB entries from 2024-07-17

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