Structure of PDB 1f2s Chain E

Receptor sequence
>1f2sE (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1f2s Crystal structure of the complex formed between bovine beta-trypsin and MCTI-A, a trypsin inhibitor of squash family, at 1.8-A resolution.
ChainE
Resolution1.79 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G193 S195 G196
Catalytic site (residue number reindexed from 1) G175 S177 G178
Enzyme Commision number 3.4.21.4: trypsin.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide E Y39 F41 C42 H57 L99 Y151 Q175 D189 S190 C191 Q192 G193 S195 S214 W215 G216 S217 Y22 F24 C25 H40 L81 Y131 Q155 D171 S172 C173 Q174 G175 S177 S192 W193 G194 S195
BS02 CA E E70 N72 V75 E80 E52 N54 V57 E62
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
GO:0097655 serpin family protein binding
Biological Process
GO:0006508 proteolysis
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0097180 serine protease inhibitor complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1f2s, PDBe:1f2s, PDBj:1f2s
PDBsum1f2s
PubMed10524768
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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