Structure of PDB 3fp7 Chain E

Receptor sequence
>3fp7E (length=223) Species: 10116 (Rattus norvegicus) [Search protein sequence]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKDSCQGDAGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN
3D structure
PDB3fp7 Structure of a serine protease poised to resynthesize a peptide bond.
ChainE
Resolution1.46 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 A195 G196
Catalytic site (residue number reindexed from 1) G175 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 peptide E H57 L99 D189 S190 C191 Q192 G193 D194 A195 S214 W215 G216 H40 L81 D171 S172 C173 Q174 G175 D176 A177 S192 W193 G194
BS02 CA E 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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fp7, PDBe:3fp7, PDBj:3fp7
PDBsum3fp7
PubMed19549826
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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