Structure of PDB 6thp Chain B Binding Site BS01

Receptor Information
>6thp Chain B (length=696) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRY
GNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGG
EPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLF
VGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVAR
LIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMT
LAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTK
LKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSE
TATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT
LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKE
DEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIV
FPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLV
DWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGG
LGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAV
NSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain6thp Chain B Residue 805 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6thp Structure-Guided Design of Substituted Biphenyl Butanoic Acid Derivatives as Neprilysin Inhibitors.
Resolution2.54 Å
Binding residue
(original residue number in PDB)		H583 H587 E646
Binding residue
(residue number reindexed from 1)		H530 H534 E593
Annotation score1
Enzymatic activity
Enzyme Commision number 3.4.24.11: neprilysin.
Gene Ontology
Molecular Function
GO:0001786 phosphatidylserine binding
GO:0004175 endopeptidase activity
GO:0004222 metalloendopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008238 exopeptidase activity
GO:0008270 zinc ion binding
GO:0042277 peptide binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0070012 oligopeptidase activity
GO:1901612 cardiolipin binding
Biological Process
GO:0001822 kidney development
GO:0001890 placenta development
GO:0006508 proteolysis
GO:0006518 peptide metabolic process
GO:0007611 learning or memory
GO:0010814 substance P catabolic process
GO:0010815 bradykinin catabolic process
GO:0016485 protein processing
GO:0019233 sensory perception of pain
GO:0030163 protein catabolic process
GO:0030324 lung development
GO:0042447 hormone catabolic process
GO:0043627 response to estrogen
GO:0046449 creatinine metabolic process
GO:0050435 amyloid-beta metabolic process
GO:0050769 positive regulation of neurogenesis
GO:0061837 neuropeptide processing
GO:0071345 cellular response to cytokine stimulus
GO:0071492 cellular response to UV-A
GO:0071493 cellular response to UV-B
GO:0090399 replicative senescence
GO:0097242 amyloid-beta clearance
GO:0150094 amyloid-beta clearance by cellular catabolic process
GO:1900273 positive regulation of long-term synaptic potentiation
Cellular Component
GO:0005737 cytoplasm
GO:0005769 early endosome
GO:0005802 trans-Golgi network
GO:0005886 plasma membrane
GO:0005903 brush border
GO:0005925 focal adhesion
GO:0008021 synaptic vesicle
GO:0009986 cell surface
GO:0016020 membrane
GO:0030424 axon
GO:0030425 dendrite
GO:0030667 secretory granule membrane
GO:0031410 cytoplasmic vesicle
GO:0043025 neuronal cell body
GO:0044306 neuron projection terminus
GO:0045121 membrane raft
GO:0045202 synapse
GO:0070062 extracellular exosome
GO:0098793 presynapse

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6thp, PDBe:6thp, PDBj:6thp
PDBsum6thp
PubMed32071687
UniProtP08473|NEP_HUMAN Neprilysin (Gene Name=MME)

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