Structure of PDB 1a0l Chain D Binding Site BS01

Receptor Information
>1a0l Chain D (length=244) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VKVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPKK
Ligand information
Ligand IDAPA
InChIInChI=1S/C10H12N2O3/c11-9(12)7-3-1-6(2-4-7)5-8(13)10(14)15/h1-4,8,13H,5H2,(H3,11,12)(H,14,15)/t8-/m0/s1
InChIKeyFAFAPKBWTCDDJC-QMMMGPOBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0[H]/N=C(/c1ccc(cc1)C[C@@H](C(=O)O)O)\N
CACTVS 3.370NC(=N)c1ccc(C[C@H](O)C(O)=O)cc1
CACTVS 3.370NC(=N)c1ccc(C[CH](O)C(O)=O)cc1
ACDLabs 12.01O=C(O)C(O)Cc1ccc(cc1)C(=[N@H])N
OpenEye OEToolkits 1.7.0c1cc(ccc1CC(C(=O)O)O)C(=N)N
FormulaC10 H12 N2 O3
Name(2S)-3-(4-carbamimidoylphenyl)-2-hydroxypropanoic acid
ChEMBL
DrugBank
ZINCZINC000015277701
PDB chain1a0l Chain D Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1a0l Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		H57 D189 S190 Q192 G193 S195 V213 W215
Binding residue
(residue number reindexed from 1)		H44 D188 S189 Q191 G192 S194 V212 W214
Annotation score1
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
Biological Process
GO:0006508 proteolysis
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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Biological Process
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Cellular Component
External links
PDB RCSB:1a0l, PDBe:1a0l, PDBj:1a0l
PDBsum1a0l
PubMed9521329
UniProtP20231|TRYB2_HUMAN Tryptase beta-2 (Gene Name=TPSB2)

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