Structure of PDB 3tgk Chain E

Receptor sequence
>3tgkE (length=217) Species: 10116 (Rattus norvegicus) [Search protein sequence]
KGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLG
EHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVA
TVALPSSCAPAGTQCLISGWGNVNEPDLLQCLDAPLLPQADCEASYPGKI
TDNMVCVGFLEGGKDSCQGNSGGPVVCNGELQGIVSWGYGCALPDNPGVY
TKVCNYVDWIQDTIAAN
3D structure
PDB3tgk The energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinity.
ChainE
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) G193 S195 G196
Catalytic site (residue number reindexed from 1) G169 S171 G172
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 E E70 N72 V75 E77 E80 E51 N53 V56 E58 E61
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3tgk, PDBe:3tgk, PDBj:3tgk
PDBsum3tgk
PubMed11420435
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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