Structure of PDB 1slx Chain B

Receptor sequence
>1slxB (length=219) Species: 10116 (Rattus norvegicus) [Search protein sequence]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKVATVA
LPSSCAPAGTQCLISGWGHTLSSGVNHPDLLQCLDAPLLPQADCEASYPG
KITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPG
VYTKVCNYVDWIQDTIAAN
3D structure
PDB1slx X-ray structures of a designed binding site in trypsin show metal-dependent geometry.
ChainB
Resolution2.2 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 Q170 G171 D172 S173 G174
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 B E70 N72 I73 V75 E77 E52 N54 I55 V57 E59
BS02 ZN B H143 H151 H119 H127
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:1slx, PDBe:1slx, PDBj:1slx
PDBsum1slx
PubMed8634241
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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