Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6XUE

Human Ecto-5'-nucleotidase (CD73) in complex with A2396 (compound 74 in publication) in the closed form in crystal form IV

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002953	molecular_function	5'-deoxynucleotidase activity
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006196	biological_process	AMP catabolic process
A	0006259	biological_process	DNA metabolic process
A	0007159	biological_process	leukocyte cell-cell adhesion
A	0008253	molecular_function	5'-nucleotidase activity
A	0008270	molecular_function	zinc ion binding
A	0009166	biological_process	nucleotide catabolic process
A	0009897	cellular_component	external side of plasma membrane
A	0009986	cellular_component	cell surface
A	0010035	biological_process	obsolete response to inorganic substance
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0033198	biological_process	response to ATP
A	0042802	molecular_function	identical protein binding
A	0046032	biological_process	ADP catabolic process
A	0046034	biological_process	ATP metabolic process
A	0046086	biological_process	adenosine biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050728	biological_process	negative regulation of inflammatory response
A	0055074	biological_process	calcium ion homeostasis
A	0070062	cellular_component	extracellular exosome
A	0098552	cellular_component	side of membrane
A	0110148	biological_process	obsolete biomineralization
A	0140928	biological_process	inhibition of non-skeletal tissue mineralization
B	0000166	molecular_function	nucleotide binding
B	0002953	molecular_function	5'-deoxynucleotidase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006196	biological_process	AMP catabolic process
B	0006259	biological_process	DNA metabolic process
B	0007159	biological_process	leukocyte cell-cell adhesion
B	0008253	molecular_function	5'-nucleotidase activity
B	0008270	molecular_function	zinc ion binding
B	0009166	biological_process	nucleotide catabolic process
B	0009897	cellular_component	external side of plasma membrane
B	0009986	cellular_component	cell surface
B	0010035	biological_process	obsolete response to inorganic substance
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0033198	biological_process	response to ATP
B	0042802	molecular_function	identical protein binding
B	0046032	biological_process	ADP catabolic process
B	0046034	biological_process	ATP metabolic process
B	0046086	biological_process	adenosine biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0050728	biological_process	negative regulation of inflammatory response
B	0055074	biological_process	calcium ion homeostasis
B	0070062	cellular_component	extracellular exosome
B	0098552	cellular_component	side of membrane
B	0110148	biological_process	obsolete biomineralization
B	0140928	biological_process	inhibition of non-skeletal tissue mineralization

Functional Information from PROSITE/UniProt

site_id	PS00785
Number of Residues	13
Details	5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. LtILHTnDvHSrL

Chain	Residue	Details
A	LEU29-LEU41

site_id	PS00786
Number of Residues	12
Details	5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. YdamaLGNHEFD

Chain	Residue	Details
A	TYR110-ASP121

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22997138","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34403084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4H1S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7P9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22997138","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34403084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4H1S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H1Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7P9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22997138","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34403084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4H1S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H1Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4H2I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7P9N","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"34403084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7PBA","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Lipidation: {"description":"GPI-anchor amidated serine","evidences":[{"source":"PubMed","id":"2129526","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22997138","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)