Structure of PDB 1slv Chain B Binding Site BS02

Receptor Information
>1slv Chain B (length=215) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKVATVA
LPSSCAPAGTQCLISGWGHTLNHPDLLQCLDAPLLPQADCEASYPGKITD
NMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPGVYTK
VCNYVDWIQDTIAAN
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain1slv Chain B Residue 248 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1slv X-ray structures of a designed binding site in trypsin show metal-dependent geometry.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		H143 H151
Binding residue
(residue number reindexed from 1)		H119 H123
Annotation score3
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 Q166 G167 D168 S169 G170
Enzyme Commision number 3.4.21.4: trypsin.
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:1slv, PDBe:1slv, PDBj:1slv
PDBsum1slv
PubMed8634241
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

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