Structure of PDB 4abj Chain A

Receptor sequence
>4abjA (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB4abj Braces for the Peptide Backbone: Insights Into Structure-Activity Relation-Ships of Protease Inhibitor Mimics with Locked Amide Conformations
ChainA
Resolution1.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H63 D107 Q197 G198 D199 S200 G201
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 peptide A F47 H63 S101 L104 Y154 D194 S195 C196 Q197 G198 S200 S215 W216 G217 F24 H40 S78 L81 Y131 D171 S172 C173 Q174 G175 S177 S192 W193 G194
BS02 CA A E75 N77 V80 E85 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

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Biological Process
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Cellular Component
External links
PDB RCSB:4abj, PDBe:4abj, PDBj:4abj
PDBsum4abj
PubMed22374650
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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