Structure of PDB 5wi6 Chain D

Receptor sequence
>5wi6D (length=243) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQCGADIALLELEEP
VNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPK
3D structure
PDB5wi6 Dual functionality of beta-tryptase protomers as both proteases and cofactors in the active tetramer.
ChainD
Resolution2.72 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
Catalytic site (residue number reindexed from 1) H44 D91 Q191 G192 D193 S194
Enzyme Commision number 3.4.21.59: tryptase.
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 0GJ D H57 D189 S190 C191 Q192 S195 S214 W215 G216 H44 D188 S189 C190 Q191 S194 S213 W214 G215
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0042802 identical protein binding
Biological Process
GO:0006508 proteolysis
GO:0006952 defense response
GO:0022617 extracellular matrix disassembly
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0062023 collagen-containing extracellular matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5wi6, PDBe:5wi6, PDBj:5wi6
PDBsum5wi6
PubMed29661938
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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