Structure of PDB 2btc Chain E

Receptor sequence

>2btcE (length=223) Species: 9913 (Bos taurus)

IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN

3D structure

• PDB: 2btc High-resolution structures of three new trypsin-squash-inhibitor complexes: a detailed comparison with other trypsins and their complexes.
• Chain: E
• Resolution: 1.5 Å

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	F41 H57 T149 Y151 D189 S190 C191 Q192 G193 S195 S214 W215 G216 S217	F24 H40 T129 Y131 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

External links

• PDB: RCSB:2btc, PDBe:2btc, PDBj:2btc
• PDBsum: 2btc
• PubMed: 10089404
• UniProt: P00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)