3EWC
Crystal Structure of adenosine deaminase from Plasmodial vivax in complex with MT-coformycin
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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 372 |
| Chain | Residue |
| A | HIS42 |
| A | HIS44 |
| A | HIS226 |
| A | ASP310 |
| A | MCF373 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE MCF A 373 |
| Chain | Residue |
| A | ILE170 |
| A | ASP172 |
| A | THR173 |
| A | GLY174 |
| A | HIS175 |
| A | GLY201 |
| A | HIS226 |
| A | GLU229 |
| A | HIS253 |
| A | ASP310 |
| A | ASP311 |
| A | ZN372 |
| A | HIS44 |
| A | LEU47 |
| A | LEU85 |
| A | PHE88 |
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 |
