Structure of PDB 1qb9 Chain A

Receptor sequence
>1qb9A (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1qb9 Crystallographic analysis of potent and selective factor Xa inhibitors complexed to bovine trypsin.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H46 D90 Q180 G181 D182 S183 G184
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 CA A E58 N60 V63 E65 E68 E52 N54 V57 E59 E62
BS02 CA A D59 E65 D53 E59
BS03 806 A N85 T86 L87 Q161 D177 S178 W199 G200 G202 N79 T80 L81 Q155 D171 S172 W193 G194 G196 MOAD: Ki=36nM
PDBbind-CN: -logKd/Ki=7.44,Ki=36nM
BindingDB: Ki=36nM
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1qb9, PDBe:1qb9, PDBj:1qb9
PDBsum1qb9
PubMed10417407
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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