Structure of PDB 6bfp Chain A

Receptor sequence
>6bfpA (length=221) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSTSYPDVLKCLKAPILSDSSCKSAY
PGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNK
PGVYTKVCNYVSWIKQTIASN
3D structure
PDB6bfp Structures of full-length plasma kallikrein bound to highly specific inhibitors describe a new mode of targeted inhibition.
ChainA
Resolution1.292 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 Q172 G173 D174 S175 G176
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 A E75 N77 V80 E85 E52 N54 V57 E62
BS02 DJY A H63 L104 Y154 D194 S195 Q197 S200 V214 S215 W216 G217 G219 H40 L81 Y129 D169 S170 Q172 S175 V189 S190 W191 G192 G194 PDBbind-CN: -logKd/Ki=7.70,IC50=0.02uM
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:6bfp, PDBe:6bfp, PDBj:6bfp
PDBsum6bfp
PubMed30876891
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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