Structure of PDB 4mpu Chain A Binding Site BS01

Receptor Information
>4mpu Chain A (length=243) 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
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVPK
Ligand information
Ligand IDX2A
InChIInChI=1S/C50H58N6O8/c51-31-33-7-1-9-37(27-33)35-15-23-55(24-16-35)43(57)39-11-3-13-41(29-39)53-45(59)49(62)48(21-6-22-48)63-50(64-49,47(61)19-5-20-47)46(60)54-42-14-4-12-40(30-42)44(58)56-25-17-36(18-26-56)38-10-2-8-34(28-38)32-52/h1-4,7-14,27-30,35-36,61-62H,5-6,15-26,31-32,51-52H2,(H,53,59)(H,54,60)/t49-,50+/m0/s1
InChIKeySNRGDRCFKQFZAO-LOYCUKJKSA-N
SMILES
SoftwareSMILES
CACTVS 3.385NCc1cccc(c1)[C@@H]2CCN(CC2)C(=O)c3cccc(NC(=O)[C@]4(O)O[C@](OC45CCC5)(C(=O)Nc6cccc(c6)C(=O)N7CC[C@@H](CC7)c8cccc(CN)c8)C9(O)CCC9)c3
CACTVS 3.385NCc1cccc(c1)[CH]2CCN(CC2)C(=O)c3cccc(NC(=O)[C]4(O)O[C](OC45CCC5)(C(=O)Nc6cccc(c6)C(=O)N7CC[CH](CC7)c8cccc(CN)c8)C9(O)CCC9)c3
OpenEye OEToolkits 1.7.6c1cc(cc(c1)C2CCN(CC2)C(=O)c3cccc(c3)NC(=O)C4(C5(CCC5)OC(O4)(C(=O)Nc6cccc(c6)C(=O)N7CCC(CC7)c8cccc(c8)CN)C9(CCC9)O)O)CN
OpenEye OEToolkits 1.7.6c1cc(cc(c1)C2CCN(CC2)C(=O)c3cccc(c3)NC(=O)[C@]4(C5(CCC5)O[C@@](O4)(C(=O)Nc6cccc(c6)C(=O)N7CCC(CC7)c8cccc(c8)CN)C9(CCC9)O)O)CN
ACDLabs 12.01O=C(N2CCC(c1cccc(c1)CN)CC2)c3cc(ccc3)NC(=O)C5(O)OC(OC45CCC4)(C(=O)Nc8cc(C(=O)N7CCC(c6cccc(c6)CN)CC7)ccc8)C9(O)CCC9
FormulaC50 H58 N6 O8
Name(6S,8R)-N,N'-bis[3-({4-[3-(aminomethyl)phenyl]piperidin-1-yl}carbonyl)phenyl]-8-hydroxy-6-(1-hydroxycyclobutyl)-5,7-dioxaspiro[3.4]octane-6,8-dicarboxamide
ChEMBL
DrugBank
ZINCZINC000205036373
PDB chain4mpu Chain B Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4mpu Target-Directed Self-Assembly of Homodimeric Drugs Against beta-Tryptase.
Resolution1.649 Å
Binding residue
(original residue number in PDB)		Q117 D218 S219 C220 Q221 W244 G245 E246 G247
Binding residue
(residue number reindexed from 1)		Q87 D188 S189 C190 Q191 W214 G215 E216 G217
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H74 D121 Q221 G222 D223 S224 G225
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4mpu, PDBe:4mpu, PDBj:4mpu
PDBsum4mpu
PubMed30128075
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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