Structure of PDB 2f9n Chain D Binding Site BS02

Receptor Information

>2f9n Chain D (length=243) Species: 9606 (Homo sapiens)

IVGGQEAPRSKWPWQVSLRVRDRYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLATLRVQLREQHLYYQDQLLPVSRIIVHPQFYIIQTGADIALLELEEP
VNISSRVHTVMLPPASETFPPGMPCWVTGWGDVDNDEPLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIIRDDMLCAGNSQRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPK

Ligand information

>2f9n Chain H (length=3) Species: 66430 (Streptomyces roseus)

LLR

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2f9n X-ray Structures of Free and Leupeptin-complexed Human alpha I-Tryptase Mutants: Indication for an alpha to beta-Tryptase Transition
• Resolution: 1.6 Å
• Binding residue (original residue number in PDB): H57 D189 S190 Q192 S195 W215 G216 G219 G226
• Binding residue (residue number reindexed from 1): H44 D188 S189 Q191 S194 W214 G215 G217 G225

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.

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

External links

• PDB: RCSB:2f9n, PDBe:2f9n, PDBj:2f9n
• PDBsum: 2f9n
• PubMed: 16414069
• UniProt: Q15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)