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1K9O

CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX

Replaces:  1I99
Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006508biological_processproteolysis
E0007584biological_processresponse to nutrient
E0007586biological_processdigestion
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0016787molecular_functionhydrolase activity
E0030574biological_processcollagen catabolic process
E0046872molecular_functionmetal ion binding
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005615cellular_componentextracellular space
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
EVAL53-CYS58

site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. VHIDRPFYFeL
ChainResidueDetails
IVAL361-LEU371

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
EHIS57
EASP102
EALA195

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
EGLU70
EASN72
EVAL75
EGLU80

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Required for specificity => ECO:0000250
ChainResidueDetails
EASP189

218853

PDB entries from 2024-04-24

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