Structure of PDB 6vvu Chain C Binding Site BS01

Receptor Information
>6vvu Chain C (length=242) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDV
KDLAALRVQLREQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEP
VNVSSHVHTVTLPPASETFPPGMPCWVTGWGDVDNDERLPPPFPLKQVKV
PIMENHICDAKYHLGAYTGDDVRIVRDDMLCAGNTRRDSCQGDSGGPLVC
KVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHYVP
Ligand information
Ligand ID0GJ
InChIInChI=1S/C14H27ClN6O5/c15-6-10(22)9(2-1-5-19-14(17)18)21-11(23)7-20-13(26)8(16)3-4-12(24)25/h8-10,22H,1-7,16H2,(H,20,26)(H,21,23)(H,24,25)(H4,17,18,19)/p+1/t8-,9-,10+/m0/s1
InChIKeyXELWNHKFCNMWQO-LPEHRKFASA-O
SMILES
SoftwareSMILES
CACTVS 3.370N[CH](CCC(O)=O)C(=O)NCC(=O)N[CH](CCCNC(N)=[NH2+])[CH](O)CCl
CACTVS 3.370N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CCCNC(N)=[NH2+])[C@H](O)CCl
ACDLabs 12.01O=C(NC(CCCNC(=[NH2+])\N)C(O)CCl)CNC(=O)C(N)CCC(=O)O
OpenEye OEToolkits 1.7.0C(CC(C(CCl)O)NC(=O)CNC(=O)C(CCC(=O)O)N)CNC(=[NH2+])N
OpenEye OEToolkits 1.7.0C(C[C@@H]([C@@H](CCl)O)NC(=O)CNC(=O)[C@H](CCC(=O)O)N)CNC(=[NH2+])N
FormulaC14 H28 Cl N6 O5
NameL-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide
ChEMBL
DrugBank
ZINC
PDB chain6vvu Chain C Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6vvu Bivalent antibody pliers inhibit beta-tryptase by an allosteric mechanism dependent on the IgG hinge.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		H57 D189 S190 C191 Q192 S195 S214 W215 G216
Binding residue
(residue number reindexed from 1)		H44 D188 S189 C190 Q191 S194 S213 W214 G215
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195
Catalytic site (residue number reindexed from 1) H44 D91 Q191 G192 D193 S194
Enzyme Commision number 3.4.21.59: tryptase.
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6vvu, PDBe:6vvu, PDBj:6vvu
PDBsum6vvu
PubMed33353951
UniProtQ15661|TRYB1_HUMAN Tryptase alpha/beta-1 (Gene Name=TPSAB1)

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