Structure of PDB 4mpv Chain B

Receptor sequence
>4mpvB (length=243) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPK
3D structure
PDB4mpv Target-Directed Self-Assembly of Homodimeric Drugs Against beta-Tryptase.
ChainB
Resolution2.305 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H74 D121 Q221 G222 D223 S224 G225
Catalytic site (residue number reindexed from 1) H44 D91 Q191 G192 D193 S194 G195
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 2A4 B Q117 S219 C220 W244 G245 G247 Q87 S189 C190 W214 G215 G217
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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Biological Process
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Cellular Component
External links
PDB RCSB:4mpv, PDBe:4mpv, PDBj:4mpv
PDBsum4mpv
PubMed30128075
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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