1DMT

STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001786	molecular_function	phosphatidylserine binding
A	0001822	biological_process	kidney development
A	0001890	biological_process	placenta development
A	0002003	biological_process	angiotensin maturation
A	0004175	molecular_function	endopeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0004222	molecular_function	metalloendopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005769	cellular_component	early endosome
A	0005802	cellular_component	trans-Golgi network
A	0005813	cellular_component	centrosome
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005903	cellular_component	brush border
A	0005925	cellular_component	focal adhesion
A	0006508	biological_process	proteolysis
A	0006518	biological_process	peptide metabolic process
A	0007611	biological_process	learning or memory
A	0008021	cellular_component	synaptic vesicle
A	0008233	molecular_function	peptidase activity
A	0008237	molecular_function	metallopeptidase activity
A	0008238	molecular_function	exopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009986	cellular_component	cell surface
A	0010814	biological_process	substance P catabolic process
A	0010815	biological_process	bradykinin catabolic process
A	0016020	cellular_component	membrane
A	0016485	biological_process	protein processing
A	0016787	molecular_function	hydrolase activity
A	0019233	biological_process	sensory perception of pain
A	0030163	biological_process	protein catabolic process
A	0030324	biological_process	lung development
A	0030424	cellular_component	axon
A	0030425	cellular_component	dendrite
A	0030667	cellular_component	secretory granule membrane
A	0031410	cellular_component	cytoplasmic vesicle
A	0036064	cellular_component	ciliary basal body
A	0042277	molecular_function	peptide binding
A	0042447	biological_process	hormone catabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0043025	cellular_component	neuronal cell body
A	0043627	biological_process	response to estrogen
A	0044306	cellular_component	neuron projection terminus
A	0045121	cellular_component	membrane raft
A	0045202	cellular_component	synapse
A	0046449	biological_process	creatinine metabolic process
A	0046872	molecular_function	metal ion binding
A	0050435	biological_process	amyloid-beta metabolic process
A	0050769	biological_process	positive regulation of neurogenesis
A	0061837	biological_process	neuropeptide processing
A	0070012	molecular_function	oligopeptidase activity
A	0070062	cellular_component	extracellular exosome
A	0071345	biological_process	cellular response to cytokine stimulus
A	0071492	biological_process	cellular response to UV-A
A	0071493	biological_process	cellular response to UV-B
A	0090399	biological_process	replicative senescence
A	0097242	biological_process	amyloid-beta clearance
A	0098793	cellular_component	presynapse
A	0150094	biological_process	amyloid-beta clearance by cellular catabolic process
A	1900273	biological_process	positive regulation of long-term synaptic potentiation
A	1901612	molecular_function	cardiolipin binding

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEITHGF

Chain	Residue	Details
A	VAL580-PHE589

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	694
Details	Domain: {"description":"Peptidase M13","evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8168535","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P07861","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01233","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10669592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14747736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17704566","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10669592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14747736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17704566","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10669592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14747736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17704566","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22766194","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1r1j

Chain	Residue	Details
A	GLU584
A	ARG717
A	HIS711
A	ASP650

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 623

Chain	Residue	Details
A	HIS583	metal ligand
A	GLU584	proton shuttle (general acid/base)
A	HIS587	metal ligand
A	GLU646	metal ligand
A	ASP650	electrostatic stabiliser
A	HIS711	electrostatic stabiliser
A	ARG717	electrostatic stabiliser

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