Structure of PDB 6vvu Chain D

Receptor sequence
>6vvuD (length=242) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVP
3D structure
PDB6vvu Bivalent antibody pliers inhibit beta-tryptase by an allosteric mechanism dependent on the IgG hinge.
ChainD
Resolution3.0 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
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:6vvu, PDBe:6vvu, PDBj:6vvu
PDBsum6vvu
PubMed33353951
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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