Structure of PDB 3aav Chain A

Receptor sequence

>3aavA (length=223) Species: 9913 (Bos taurus)

IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN

3D structure

• PDB: 3aav Structural basis for the design of novel Schiff base metal chelate inhibitors of trypsin
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H40 D84 Q174 G175 D176 S177 G178
• Catalytic site (residue number reindexed from 1): H40 D84 Q174 G175 D176 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	A2C	A	F24 H40 D171 S172 C173 G175 D176 S177 V191 G196 C197	F24 H40 D171 S172 C173 G175 D176 S177 V191 G196 C197	PDBbind-CN: -logKd/Ki=6.62,Ki=0.24uM
BS02	CA	A	E52 N54 V57 E62	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:3aav, PDBe:3aav, PDBj:3aav
• PDBsum: 3aav
• PubMed: 20202854
• UniProt: P00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)