Structure of PDB 1j15 Chain A

Receptor sequence
>1j15A (length=223) Species: 10116 (Rattus norvegicus) [Search protein sequence]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRETYNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SSSFIITDNMVCVGFLEGGKDACQGDSGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN
3D structure
PDB1j15 Reconstructing the Binding Site of Factor Xa in Trypsin Reveals Ligand-induced Structural Plasticity
ChainA
Resolution2.0 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 E77 E80 E52 N54 V57 E59 E62
BS02 BEN A D189 A190 C191 Q192 V213 W215 G216 G219 D171 A172 C173 Q174 V191 W193 G194 G196 MOAD: Ki=143uM
PDBbind-CN: -logKd/Ki=3.84,Ki=143uM
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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Cellular Component
External links
PDB RCSB:1j15, PDBe:1j15, PDBj:1j15
PDBsum1j15
PubMed12527302
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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