Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4H1Y

Human ecto-5'-nucleotidase (CD73): crystal form II (open) in complex with PSB11552

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0000166	molecular_function	nucleotide binding
P	0002953	molecular_function	5'-deoxynucleotidase activity
P	0005515	molecular_function	protein binding
P	0005654	cellular_component	nucleoplasm
P	0005829	cellular_component	cytosol
P	0005886	cellular_component	plasma membrane
P	0006196	biological_process	AMP catabolic process
P	0006259	biological_process	DNA metabolic process
P	0007159	biological_process	leukocyte cell-cell adhesion
P	0008252	molecular_function	nucleotidase activity
P	0008253	molecular_function	5'-nucleotidase activity
P	0008270	molecular_function	zinc ion binding
P	0009166	biological_process	nucleotide catabolic process
P	0009897	cellular_component	external side of plasma membrane
P	0009986	cellular_component	cell surface
P	0010035	biological_process	obsolete response to inorganic substance
P	0016020	cellular_component	membrane
P	0016787	molecular_function	hydrolase activity
P	0016788	molecular_function	hydrolase activity, acting on ester bonds
P	0033198	biological_process	response to ATP
P	0042802	molecular_function	identical protein binding
P	0046032	biological_process	ADP catabolic process
P	0046034	biological_process	ATP metabolic process
P	0046086	biological_process	adenosine biosynthetic process
P	0046872	molecular_function	metal ion binding
P	0050340	molecular_function	thymidylate 5'-phosphatase activity
P	0050483	molecular_function	IMP 5'-nucleotidase activity
P	0050484	molecular_function	GMP 5'-nucleotidase activity
P	0050728	biological_process	negative regulation of inflammatory response
P	0055074	biological_process	calcium ion homeostasis
P	0070062	cellular_component	extracellular exosome
P	0098552	cellular_component	side of membrane
P	0106411	molecular_function	XMP 5'-nucleosidase activity
P	0110148	biological_process	obsolete biomineralization
P	0140928	biological_process	inhibition of non-skeletal tissue mineralization

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN P 601

Chain	Residue
P	ASP36
P	ASP85
P	ASN117
P	HIS220
P	HIS243
P	ZN602
P	HOH733

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN P 602

Chain	Residue
P	ASP85
P	ZN601
P	HOH733
P	HOH769
P	HOH1055
P	ASP36
P	HIS38

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 0YQ P 603

Chain	Residue
P	GLN231
P	ASP270
P	ARG354
P	ASN390
P	GLY392
P	GLY393
P	ARG395
P	PHE417
P	GLY447
P	PHE500
P	ASP506
P	HOH954
P	HOH1082

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL P 604

Chain	Residue
P	TYR96
P	LYS326
P	LYS330
P	LYS464
P	HOH957

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL P 605

Chain	Residue
P	PHE223
P	GLU224
P	HOH971
P	HOH977
P	HOH1314

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA P 606

Chain	Residue
P	ASN213
P	ASP237
P	GLY298
P	HOH734
P	HOH892
P	HOH1081

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
P	LEU29-LEU41

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

Chain	Residue	Details
P	TYR110-ASP121

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
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
P	ASP36

site_id	SWS_FT_FI2
Number of Residues	1
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
P	HIS38

site_id	SWS_FT_FI3
Number of Residues	4
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
P	ASP85
P	ASN117
P	HIS220
P	HIS243

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:34403084, ECO:0007744\|PDB:7PBA

Chain	Residue	Details
P	ARG354
P	ASN390
P	ARG395
P	PHE417
P	PHE500
P	ASP506

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000269\|PubMed:23142347

Chain	Residue	Details
P	HIS118

site_id	SWS_FT_FI6
Number of Residues	1
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:23142347

Chain	Residue	Details
P	ASP121

site_id	SWS_FT_FI7
Number of Residues	1
Details	LIPID: GPI-anchor amidated serine => ECO:0000269\|PubMed:2129526

Chain	Residue	Details
P	SER549

site_id	SWS_FT_FI8
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
P	ASP53

site_id	SWS_FT_FI9
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:22997138, ECO:0000269\|PubMed:23142347

Chain	Residue	Details
P	ASP311

site_id	SWS_FT_FI10
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19349973

Chain	Residue	Details
P	ASP333

site_id	SWS_FT_FI11
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218

Chain	Residue	Details
P	ASP403

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