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7RTG

Crystal Structure of the Human Adenosine Deaminase 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001666biological_processresponse to hypoxia
A0004000molecular_functionadenosine deaminase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006154biological_processadenosine catabolic process
A0006196biological_processAMP catabolic process
A0006805biological_processxenobiotic metabolic process
A0007155biological_processcell adhesion
A0008270molecular_functionzinc ion binding
A0009117biological_processnucleotide metabolic process
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0009897cellular_componentexternal side of plasma membrane
A0009986cellular_componentcell surface
A0010035biological_processobsolete response to inorganic substance
A0014074biological_processresponse to purine-containing compound
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019239molecular_functiondeaminase activity
A0031410cellular_componentcytoplasmic vesicle
A0032261biological_processpurine nucleotide salvage
A0033632biological_processregulation of cell-cell adhesion mediated by integrin
A0042110biological_processT cell activation
A0043101biological_processpurine-containing compound salvage
A0043103biological_processhypoxanthine salvage
A0045187biological_processregulation of circadian sleep/wake cycle, sleep
A0046059biological_processdAMP catabolic process
A0046085biological_processadenosine metabolic process
A0046103biological_processinosine biosynthetic process
A0046872molecular_functionmetal ion binding
A0046936molecular_function2'-deoxyadenosine deaminase activity
A0060169biological_processnegative regulation of adenosine receptor signaling pathway
A0060205cellular_componentcytoplasmic vesicle lumen
A0070161cellular_componentanchoring junction
A0110148biological_processobsolete biomineralization
B0001666biological_processresponse to hypoxia
B0004000molecular_functionadenosine deaminase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006154biological_processadenosine catabolic process
B0006196biological_processAMP catabolic process
B0006805biological_processxenobiotic metabolic process
B0007155biological_processcell adhesion
B0008270molecular_functionzinc ion binding
B0009117biological_processnucleotide metabolic process
B0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
B0009897cellular_componentexternal side of plasma membrane
B0009986cellular_componentcell surface
B0010035biological_processobsolete response to inorganic substance
B0014074biological_processresponse to purine-containing compound
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019239molecular_functiondeaminase activity
B0031410cellular_componentcytoplasmic vesicle
B0032261biological_processpurine nucleotide salvage
B0033632biological_processregulation of cell-cell adhesion mediated by integrin
B0042110biological_processT cell activation
B0043101biological_processpurine-containing compound salvage
B0043103biological_processhypoxanthine salvage
B0045187biological_processregulation of circadian sleep/wake cycle, sleep
B0046059biological_processdAMP catabolic process
B0046085biological_processadenosine metabolic process
B0046103biological_processinosine biosynthetic process
B0046872molecular_functionmetal ion binding
B0046936molecular_function2'-deoxyadenosine deaminase activity
B0060169biological_processnegative regulation of adenosine receptor signaling pathway
B0060205cellular_componentcytoplasmic vesicle lumen
B0070161cellular_componentanchoring junction
B0110148biological_processobsolete biomineralization
Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
ChainResidueDetails
ASER291-PRO297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues34
DetailsRegion: {"description":"Required for binding to DDP4","evidences":[{"source":"PubMed","id":"15016824","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P03958","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"AUG-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human adenosine deaminase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2009","submissionDatabase":"PDB data bank","title":"The crystal structure of human adenosine deaminase.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3IAR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Important for interaction with adenosine receptors and increasing their affinity for agonists","evidences":[{"source":"PubMed","id":"23193172","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P03958","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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