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2F3C

Crystal structure of infestin 1, a Kazal-type serineprotease inhibitor, 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
E0008236molecular_functionserine-type peptidase activity
E0046872molecular_functionmetal ion binding
E0097180cellular_componentserine protease inhibitor complex
E0097655molecular_functionserpin family protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 239
ChainResidue
ETYR20
ETHR21
ESER107
EALA108

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 240
ChainResidue
EVAL17
ELYS140
ESER141
ESER142

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 I 103
ChainResidue
ITYR23
ISER24
ITHR28
IHOH112
ETHR144

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 241
ChainResidue
EASN92
ETHR95
EASN97
EASN98
ELYS154

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 242
ChainResidue
EGLU67
EASN69
EVAL72
EGLU74
EGLU77
EHOH261

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
EVAL51-CYS56

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV
ChainResidueDetails
EASP186-VAL197

site_idPS00282
Number of Residues24
DetailsKAZAL_1 Kazal serine protease inhibitors family signature. CprvlHrvCgSdgntYsnpCtldC
ChainResidueDetails
ICYS8-CYS31

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
ELYS58
ELEU102
EPRO195

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING:
ChainResidueDetails
EILE70
EVAL72
EGLY75
EILE80
EGLN189
ESER192
EPRO195

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
EASP99
EHIS55

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER192
EGLY193

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER192
EGLY190

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER192
EASP99
EHIS55

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER192
EASP99
EHIS55
EGLY190

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ESER192
EGLY193
EASP99
EHIS55

223790

PDB entries from 2024-08-14

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