Structure of PDB 6xvp Chain A

Receptor sequence
>6xvpA (length=696) Species: 9606 (Homo sapiens) [Search protein sequence]
GICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRY
GNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGG
EPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLF
VGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVAR
LIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMT
LAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTK
LKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSE
TATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQT
LDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKE
DEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIV
FPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLV
DWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGG
LGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAV
NSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
3D structure
PDB6xvp Molecular Basis for Omapatrilat and Sampatrilat Binding to Neprilysin-Implications for Dual Inhibitor Design with Angiotensin-Converting Enzyme.
ChainA
Resolution2.65 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.24.11: neprilysin.
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 ZN A H583 H587 E646 H530 H534 E593
BS02 D0Z A R102 F106 D107 R110 N542 A543 F544 H583 E584 H587 E646 W693 H711 R717 R49 F53 D54 R57 N489 A490 F491 H530 E531 H534 E593 W640 H658 R664 BindingDB: IC50=8.0nM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6xvp, PDBe:6xvp, PDBj:6xvp
PDBsum6xvp
PubMed32337993
UniProtP08473|NEP_HUMAN Neprilysin (Gene Name=MME)

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