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3D65

Crystal structure of Textilinin-1, a Kunitz-type serine protease inhibitor from the Australian Common Brown snake venom, in complex with trypsin

Functional Information from GO Data
ChainGOidnamespacecontents
E0004175molecular_functionendopeptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0006508biological_processproteolysis
E0007586biological_processdigestion
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0016787molecular_functionhydrolase activity
E0046872molecular_functionmetal ion binding
E0097180cellular_componentserine protease inhibitor complex
E0097655molecular_functionserpin family protein binding
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0030414molecular_functionpeptidase inhibitor activity
I0044469biological_processvenom-mediated blood coagulation
I0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA E 1
ChainResidue
EGLU70
EASN72
EGLU80
EHOH256
EHOH268

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
EVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
EASP189-VAL200

site_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FiyGGCegnannFitkeeC
ChainResidueDetails
IPHE35-CYS53

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond for trypsin => ECO:0000250
ChainResidueDetails
IARG17
ELEU105
EPRO198

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
EILE73
EVAL75
EGLY78
EILE83
EGLN192
ESER195
EPRO198

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
ESER195
EHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
EHIS57

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EGLY193

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER195
EGLY196

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
ESER195
EGLY193
EHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP102
ESER195
EHIS57
EGLY196

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PDB entries from 2025-06-11

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