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Structure of PDB 1v2k Chain T

Receptor sequence >1v2kT (length=223) Species: 9913 (Bos taurus) [Search protein sequence] IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL GEDNINVVEGNEQFISASKSIVHPSYNSETYNNDIMLIKLKSAASLNSRV ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS ASSFIITSNMFCAGYLEGGKDACQGDSGGPVVCSGKLQGIVSWGEGCAQK NKPGVYTKVCNYVSWIKQTIASN

3D structure PDB 1v2k Understanding protein-ligand interactions: the price of protein flexibility Chain T Resolution 2.0 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

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 CA T E70 N72 V75 E80 E52 N54 V57 E62 BS02 ZEN T Y99 F174 A190 Q192 V213 W215 G216 G219 C220 V227 Y228 Y81 F154 A172 Q174 V191 W193 G194 G196 C197 V205 Y206 MOAD: Ki=0.65uM PDBbind-CN: -logKd/Ki=6.19,Ki=0.65uM

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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