Structure of PDB 3v7t Chain B

Receptor sequence
>3v7tB (length=242) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVP
3D structure
PDB3v7t A beta-tryptase inhibitor with a tropanylamide scaffold to improve in vitro stability and to lower hERG channel binding affinity
ChainB
Resolution2.09 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H59 D106 Q206 G207 D208 S209 G210
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 0GX B Q102 D203 S204 C205 Q206 S209 V227 W229 G230 G232 C233 Q87 D188 S189 C190 Q191 S194 V212 W214 G215 G217 C218 MOAD: Ki=62nM
BS02 CO3 B H59 Q206 S209 H44 Q191 S194
BS03 0GX B P63 Y99 P48 Y84 MOAD: Ki=62nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
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:3v7t, PDBe:3v7t, PDBj:3v7t
PDBsum3v7t
PubMed22264487
UniProtP20231|TRYB2_HUMAN Tryptase beta-2 (Gene Name=TPSB2)

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