Structure of PDB 2tpi Chain Z

Receptor sequence

>2tpiZ (length=220) Species: 9913 (Bos taurus)

GYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGED
NINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASI
SLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYP
GQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKP
GVYTKVCNYVSWIKQTIASN

3D structure

• PDB: 2tpi Structure of the Complex Formed by Bovine Trypsin and Bovine Pancreatic Trypsin Inhibitor. II. Crystallographic Refinement at 1.9 Angstroms Resolution
• Chain: Z
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): G193 S195 G196
• Catalytic site (residue number reindexed from 1): G172 S174 G175
• 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	ILE	Z	I138 G142 N143 T144 K156 D189 D194	I115 G119 N120 T121 K133 D168 D173	PDBbind-CN: -logKd/Ki=4.31,Kd=49uM
BS02	VAL	Z	G19 T144 K188 D189	G1 T121 K167 D168	PDBbind-CN: -logKd/Ki=4.31,Kd=49uM

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:2tpi, PDBe:2tpi, PDBj:2tpi
• PDBsum: 2tpi
• UniProt: P00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)