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6TVE

Unliganded human CD73 (5'-nucleotidase) in the open state

Functional Information from GO Data
ChainGOidnamespacecontents
P0000166molecular_functionnucleotide binding
P0002953molecular_function5'-deoxynucleotidase activity
P0005515molecular_functionprotein binding
P0005654cellular_componentnucleoplasm
P0005829cellular_componentcytosol
P0005886cellular_componentplasma membrane
P0006196biological_processAMP catabolic process
P0006259biological_processDNA metabolic process
P0007159biological_processleukocyte cell-cell adhesion
P0008253molecular_function5'-nucleotidase activity
P0008270molecular_functionzinc ion binding
P0009166biological_processnucleotide catabolic process
P0009897cellular_componentexternal side of plasma membrane
P0009986cellular_componentcell surface
P0010035biological_processobsolete response to inorganic substance
P0016020cellular_componentmembrane
P0016787molecular_functionhydrolase activity
P0016788molecular_functionhydrolase activity, acting on ester bonds
P0033198biological_processresponse to ATP
P0042802molecular_functionidentical protein binding
P0046032biological_processADP catabolic process
P0046034biological_processATP metabolic process
P0046086biological_processadenosine biosynthetic process
P0046872molecular_functionmetal ion binding
P0050728biological_processnegative regulation of inflammatory response
P0055074biological_processcalcium ion homeostasis
P0070062cellular_componentextracellular exosome
P0098552cellular_componentside of membrane
P0110148biological_processobsolete biomineralization
P0140928biological_processinhibition of non-skeletal tissue mineralization
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA P 601
ChainResidue
PASN213
PASP237
PGLY298
PHOH771
PHOH991
PHOH1116

site_idAC2
Number of Residues7
Detailsbinding site for residue ZN P 602
ChainResidue
PHIS220
PHIS243
PZN603
PHOH733
PASP36
PASP85
PASN117

site_idAC3
Number of Residues7
Detailsbinding site for residue ZN P 603
ChainResidue
PASP36
PHIS38
PASP85
PSER520
PZN602
PHOH733
PHOH741

site_idAC4
Number of Residues6
Detailsbinding site for residue DMS P 604
ChainResidue
PPHE65
PARG72
PALA107
PLEU108
PARG109
PHOH959

site_idAC5
Number of Residues10
Detailsbinding site for residue GOL P 605
ChainResidue
PGLN88
PASP121
PASN122
PASN371
PASP522
PASN526
PTHR530
PHOH954
PHOH957
PHOH1169

site_idAC6
Number of Residues6
Detailsbinding site for residue DMS P 606
ChainResidue
PARG72
PARG73
PALA74
PPRO76
PPRO149
PGLN153

site_idAC7
Number of Residues5
Detailsbinding site for residue DMS P 607
ChainResidue
PTYR334
PGLN337
PGLU338
PLEU339
PHOH721

site_idAC8
Number of Residues5
Detailsbinding site for residue DMS P 608
ChainResidue
PTYR281
PASN499
PASN503
PHOH772
PHOH1202

site_idAC9
Number of Residues7
Detailsbinding site for residue DMS P 609
ChainResidue
PARG40
PASP47
PPHE417
PASN499
PPHE500
PHOH881
PHOH1200

site_idAD1
Number of Residues3
Detailsbinding site for residue GOL P 610
ChainResidue
PTYR96
PTRP327
PHOH701

site_idAD2
Number of Residues6
Detailsbinding site for residue DMS P 611
ChainResidue
PMET535
PILE538
PTYR539
PPRO540
PHOH962
PHOH1117

site_idAD3
Number of Residues8
Detailsbinding site for residue GOL P 612
ChainResidue
PVAL78
PLEU79
PASP111
PPRO165
PVAL166
PGLY167
PHOH893
PHOH934

site_idAD4
Number of Residues4
Detailsbinding site for residue DMS P 613
ChainResidue
PSER155
PGLY156
PTYR158
PHOH1006

site_idAD5
Number of Residues9
Detailsbinding site for residue DMS P 614
ChainResidue
PHIS456
PGLU543
PGLU543
PGLY544
PGLY544
PLYS547
PLYS547
PHOH1151
PHOH1151

Functional Information from PROSITE/UniProt
site_idPS00785
Number of Residues13
Details5_NUCLEOTIDASE_1 5'-nucleotidase signature 1. LtILHTnDvHSrL
ChainResidueDetails
PLEU29-LEU41

site_idPS00786
Number of Residues12
Details5_NUCLEOTIDASE_2 5'-nucleotidase signature 2. YdamaLGNHEFD
ChainResidueDetails
PTYR110-ASP121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34403084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7PBA","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"23142347","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsLipidation: {"description":"GPI-anchor amidated serine","evidences":[{"source":"PubMed","id":"2129526","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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