Structure of PDB 3ljo Chain A

Receptor sequence

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

IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN

3D structure

• PDB: 3ljo Congeneric but still distinct: how closely related trypsin ligands exhibit different thermodynamic and structural properties.
• Chain: A
• Resolution: 1.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H57 D102 Q192 G193 D194 S195 G196
• 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	11U	A	L99 D189 S190 C191 V213 W215 G216 S217 G219	L81 D171 S172 C173 V191 W193 G194 S195 G196	MOAD: Kd=239nM PDBbind-CN: -logKd/Ki=6.62,Kd=239nM
BS02	CA	A	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:3ljo, PDBe:3ljo, PDBj:3ljo
• PDBsum: 3ljo
• PubMed: 21111747
• UniProt: P00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)