Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H1S

Crystal Structure of a Truncated Soluble form of Human CD73 with Ecto-5'-Nucleotidase activity

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	0008252	molecular_function	nucleotidase activity
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	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	0050340	molecular_function	thymidylate 5'-phosphatase activity
A	0050483	molecular_function	IMP 5'-nucleotidase activity
A	0050484	molecular_function	GMP 5'-nucleotidase activity
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	0106411	molecular_function	XMP 5'-nucleosidase activity
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	0008252	molecular_function	nucleotidase activity
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	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	0050340	molecular_function	thymidylate 5'-phosphatase activity
B	0050483	molecular_function	IMP 5'-nucleotidase activity
B	0050484	molecular_function	GMP 5'-nucleotidase activity
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	0106411	molecular_function	XMP 5'-nucleosidase activity
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: BINDING => ECO:0000269\|PubMed:22997138, ECO:0000269\|PubMed:23142347, ECO:0000269\|PubMed:34403084, ECO:0007744\|PDB:4H1S, ECO:0007744\|PDB:7P9N

Chain	Residue	Details
A	ASP36
B	ASP36

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22997138, ECO:0000269\|PubMed:23142347, ECO:0000269\|PubMed:34403084, ECO:0007744\|PDB:4H1S, ECO:0007744\|PDB:4H1Y, ECO:0007744\|PDB:4H2B, ECO:0007744\|PDB:4H2G, ECO:0007744\|PDB:4H2I, ECO:0007744\|PDB:7P9N

Chain	Residue	Details
A	HIS38
B	HIS38

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:22997138, ECO:0000269\|PubMed:23142347, ECO:0000269\|PubMed:34403084, ECO:0007744\|PDB:4H1S, ECO:0007744\|PDB:4H1Y, ECO:0007744\|PDB:4H2B, ECO:0007744\|PDB:4H2F, ECO:0007744\|PDB:4H2G, ECO:0007744\|PDB:4H2I, ECO:0007744\|PDB:7P9N

Chain	Residue	Details
A	ASP85
A	ASN117
A	HIS220
A	HIS243
B	ASP85
B	ASN117
B	HIS220
B	HIS243

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:34403084, ECO:0007744\|PDB:7PBA

Chain	Residue	Details
A	ARG354
B	PHE417
B	PHE500
B	ASP506
A	ASN390
A	ARG395
A	PHE417
A	PHE500
A	ASP506
B	ARG354
B	ASN390
B	ARG395

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000269\|PubMed:23142347

Chain	Residue	Details
A	HIS118
B	HIS118

site_id	SWS_FT_FI6
Number of Residues	2
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:23142347

Chain	Residue	Details
A	ASP121
B	ASP121

site_id	SWS_FT_FI7
Number of Residues	2
Details	LIPID: GPI-anchor amidated serine => ECO:0000269\|PubMed:2129526

Chain	Residue	Details
A	SER549
B	SER549

site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN53
B	ASN53

site_id	SWS_FT_FI9
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:22997138, ECO:0000269\|PubMed:23142347

Chain	Residue	Details
A	ASN311
B	ASN311

site_id	SWS_FT_FI10
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19349973

Chain	Residue	Details
A	ASN333
B	ASN333

site_id	SWS_FT_FI11
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218

Chain	Residue	Details
A	ASN403
B	ASN403

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