Structure of PDB 4a6l Chain D

Receptor sequence
>4a6lD (length=242) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVP
3D structure
PDB4a6l Structure-Based Library Design and the Discovery of a Potent and Selective Mast Cell Beta-Tryptase Inhibitor as an Oral Therapeutic Agent.
ChainD
Resolution2.05 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 D109 Q210 G211 D212 S213 G214
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 P43 D V261 P262 V241 P242 MOAD: Ki=10nM
BS02 P43 D P63 Y102 P48 Y84 MOAD: Ki=10nM
BS03 P43 D Y181 I193 D207 S208 S213 V231 W233 G234 E235 G237 Y162 I174 D188 S189 S194 V212 W214 G215 E216 G217 MOAD: Ki=10nM
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4a6l, PDBe:4a6l, PDBj:4a6l
PDBsum4a6l
PubMed22192588
UniProtP20231|TRYB2_HUMAN Tryptase beta-2 (Gene Name=TPSB2)

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