Structure of PDB 1k1l Chain A

Receptor sequence
>1k1lA (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1k1l Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 CA A E70 N72 V75 E80 E52 N54 V57 E62
BS02 FD3 A L99 D189 S190 C191 Q192 W215 G216 S217 G219 L81 D171 S172 C173 Q174 W193 G194 S195 G196 MOAD: Kd=125nM
PDBbind-CN: -logKd/Ki=6.90,Kd=125nM
BindingDB: Ki=220nM
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:1k1l, PDBe:1k1l, PDBj:1k1l
PDBsum1k1l
PubMed11676542
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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