Structure of PDB 1ylc Chain A

Receptor sequence
>1ylcA (length=223) Species: 10116 (Rattus norvegicus) [Search protein sequence]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKDSCQGDAGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN
3D structure
PDB1ylc Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin
ChainA
Resolution1.7 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 A195 G196
Catalytic site (residue number reindexed from 1) H40 D84 Q174 G175 D176 A177 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 E77 E80 E52 N54 V57 E59 E62
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007584 response to nutrient
GO:0007586 digestion
GO:0030574 collagen catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Biological Process
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Cellular Component
External links
PDB RCSB:1ylc, PDBe:1ylc, PDBj:1ylc
PDBsum1ylc
PubMed18054043
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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