Structure of PDB 2zec Chain A

Receptor sequence
>2zecA (length=242) Species: 9606 (Homo sapiens) [Search protein sequence]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVP
3D structure
PDB2zec Potent, nonpeptide inhibitors of human mast cell tryptase. Synthesis and biological evaluation of novel spirocyclic piperidine amide derivatives
ChainA
Resolution2.059 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H59 D106 Q206 G207 D208 S209 G210
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 11N A D203 S204 C205 Q206 S209 V227 W229 G230 G232 D188 S189 C190 Q191 S194 V212 W214 G215 G217
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2zec, PDBe:2zec, PDBj:2zec
PDBsum2zec
PubMed18272363
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

[Back to BioLiP]