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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 Residues2
DetailsACT_SITE: Proton donor => ECO:0000305
ChainResidueDetails
AGLU333
BGLU333

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AHIS358
BHIS358

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AHIS86
BHIS86
BHIS88
BASP89
BTRP178
BHIS267
BGLY300
BHIS330
BASP415
BASP416
AHIS88
AASP89
ATRP178
AHIS267
AGLY300
AHIS330
AASP415
AASP416

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20147294
ChainResidueDetails
AASN101
AASN159
BASN101
BASN159

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN148
BASN148

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20147294
ChainResidueDetails
AASN352
BASN352

224572

PDB entries from 2024-09-04

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