Structure of PDB 2f9n Chain C

Receptor sequence
>2f9nC (length=243) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLATLRVQLREQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEP
VNISSRVHTVMLPPASETFPPGMPCWVTGWGDVDNDEPLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIIRDDMLCAGNSQRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPK
3D structure
PDB2f9n X-ray Structures of Free and Leupeptin-complexed Human alpha I-Tryptase Mutants: Indication for an alpha to beta-Tryptase Transition
ChainC
Resolution1.6 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 peptide C H57 D189 S190 C191 Q192 S195 W215 G216 G219 H44 D188 S189 C190 Q191 S194 W214 G215 G217
BS02 BU3 C Q221A P222 R224 Q220 P221 R223
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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Molecular Function
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Cellular Component
External links
PDB RCSB:2f9n, PDBe:2f9n, PDBj:2f9n
PDBsum2f9n
PubMed16414069
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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