2PGF
Crystal structure of adenosine deaminase from Plasmodium vivax in complex with adenosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004000 | molecular_function | adenosine deaminase activity |
A | 0006166 | biological_process | purine ribonucleoside salvage |
A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019239 | molecular_function | deaminase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0046936 | molecular_function | 2'-deoxyadenosine deaminase activity |
A | 0090614 | molecular_function | 5'-methylthioadenosine deaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 401 |
Chain | Residue |
A | HIS42 |
A | HIS44 |
A | HIS226 |
A | HIS253 |
A | ASP310 |
A | ADN501 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADN A 501 |
Chain | Residue |
A | PHE88 |
A | ILE170 |
A | ASP172 |
A | GLY201 |
A | HIS226 |
A | GLU229 |
A | HIS253 |
A | ASP310 |
A | ASP311 |
A | ZN401 |
A | HOH642 |
A | HOH649 |
A | HIS44 |
A | ASP46 |
A | LEU85 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CCN A 601 |
Chain | Residue |
A | VAL149 |
A | LYS153 |
A | HOH666 |
A | HOH805 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CCN A 602 |
Chain | Residue |
A | GLN261 |
A | LYS268 |
A | ALA301 |
A | HOH658 |
Functional Information from PROSITE/UniProt
site_id | PS00485 |
Number of Residues | 7 |
Details | A_DEAMINASE Adenosine and AMP deaminase signature. SVNSDDP |
Chain | Residue | Details |
A | SER306-PRO312 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:3EWC, ECO:0007744|PDB:3EWD |
Chain | Residue | Details |
A | HIS42 | |
A | HIS44 | |
A | HIS226 | |
A | HIS253 | |
A | ASP310 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWC |
Chain | Residue | Details |
A | ASP172 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWD |
Chain | Residue | Details |
A | GLY201 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18602399, ECO:0000269|PubMed:19728741, ECO:0007744|PDB:2PGF, ECO:0007744|PDB:2PGR, ECO:0007744|PDB:2QVN, ECO:0007744|PDB:3EWC, ECO:0007744|PDB:3EWD |
Chain | Residue | Details |
A | GLU229 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity for S-methyl-5'-thioadenosine => ECO:0000269|PubMed:19728741 |
Chain | Residue | Details |
A | ASP172 |