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

1TFX

COMPLEX OF THE SECOND KUNITZ DOMAIN OF TISSUE FACTOR PATHWAY INHIBITOR WITH PORCINE TRYPSIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006508biological_processproteolysis
A0007586biological_processdigestion
A0008236molecular_functionserine-type peptidase activity
A0046872molecular_functionmetal ion binding
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006508biological_processproteolysis
B0007586biological_processdigestion
B0008236molecular_functionserine-type peptidase activity
B0046872molecular_functionmetal ion binding
C0004867molecular_functionserine-type endopeptidase inhibitor activity
D0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1007
ChainResidue
AGLU70
AASN72
AVAL75
AGLU77
AGLU80

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 4007
ChainResidue
BGLU80
BHOH5053
BGLU70
BASN72
BVAL75
BGLU77

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_idPS00280
Number of Residues19
DetailsBPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FkyGGClgnmnnFetleeC
ChainResidueDetails
CPHE33-CYS51

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive bond
ChainResidueDetails
CARG15
DARG15
ASER195
BHIS57
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19017259, ECO:0000269|PubMed:8639592
ChainResidueDetails
CASN25
DASN25
AVAL75
AGLU80
BGLU70
BASN72
BVAL75
BGLU80

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Required for specificity => ECO:0000250
ChainResidueDetails
AASP189
BASP189

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon