Structure of PDB 2f9p Chain B

Receptor sequence
>2f9pB (length=243) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLATLRVQLREQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEP
VNISSRVHTVMLPPASETFPPGMPCWVTGWGDVDNDEPLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIIRDDMLCAGNSQRDSCKGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPK
3D structure
PDB2f9p X-ray Structures of Free and Leupeptin-complexed Human alpha I-Tryptase Mutants: Indication for an alpha to beta-Tryptase Transition
ChainB
Resolution2.3 Å
3D
structure
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Enzymatic activity
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 B H57 D189 S190 S195 W215 G216 G219 H44 D188 S189 S194 W214 G215 G217
BS02 peptide B I96 I97 I85 I86
BS03 BU3 B 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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Cellular Component
External links
PDB RCSB:2f9p, PDBe:2f9p, PDBj:2f9p
PDBsum2f9p
PubMed16414069
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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