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3LGD

Crystal structure of human adenosine deaminase growth factor, adenosine deaminase type 2 (ADA2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004000molecular_functionadenosine deaminase activity
A0005615cellular_componentextracellular space
A0006154biological_processadenosine catabolic process
A0019239molecular_functiondeaminase activity
B0004000molecular_functionadenosine deaminase activity
B0005615cellular_componentextracellular space
B0006154biological_processadenosine catabolic process
B0019239molecular_functiondeaminase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues140
DetailsRegion: {"description":"Dimerization"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues116
DetailsRegion: {"description":"PRB domain"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues30
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20147294","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147294","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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