Structure of PDB 2bm2 Chain A

Receptor sequence
>2bm2A (length=242) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVP
3D structure
PDB2bm2 Structure Based Design of 4-(3-Aminomethylphenyl) Piperidinyl-1-Amides: Novel, Potent, Selective, and Orally Bioavailable Inhibitors of Bii Tryptase
ChainA
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) 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 PM2 A D189 S190 C191 V213 W215 G216 E217 G219 C220 D188 S189 C190 V212 W214 G215 E216 G217 C218 MOAD: Ki=15nM
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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Cellular Component
External links
PDB RCSB:2bm2, PDBe:2bm2, PDBj:2bm2
PDBsum2bm2
PubMed15781396
UniProtP20231|TRYB2_HUMAN Tryptase beta-2 (Gene Name=TPSB2)

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