6II7
Crystal structure of Plasmodium falciparum adenosine deaminase C27Q+L227I mutant co-complexed with Zn ion, hypoxanthine and inosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004000 | molecular_function | adenosine deaminase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006154 | biological_process | adenosine catabolic process |
A | 0006166 | biological_process | purine ribonucleoside salvage |
A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019239 | molecular_function | deaminase activity |
A | 0043103 | biological_process | hypoxanthine salvage |
A | 0046103 | biological_process | inosine biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0046936 | molecular_function | 2'-deoxyadenosine deaminase activity |
A | 0060169 | biological_process | negative regulation of adenosine receptor signaling pathway |
A | 0090614 | molecular_function | 5'-methylthioadenosine deaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue NOS A 401 |
Chain | Residue |
A | HIS48 |
A | ALA204 |
A | GLY205 |
A | ASP315 |
A | MET318 |
A | HPA402 |
A | HOH501 |
A | HOH505 |
A | HOH513 |
A | HOH560 |
A | ASP50 |
A | VAL51 |
A | ALA96 |
A | SER133 |
A | PHE136 |
A | THR174 |
A | GLY175 |
A | ASP176 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue HPA A 402 |
Chain | Residue |
A | HIS48 |
A | LEU89 |
A | VAL93 |
A | GLY205 |
A | GLU233 |
A | HIS257 |
A | ASP314 |
A | ASP315 |
A | NOS401 |
A | ZN403 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | HIS46 |
A | HIS48 |
A | HIS230 |
A | ASP314 |
A | HPA402 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue ZN A 404 |
Chain | Residue |
A | ASP144 |
A | ASP146 |
A | ASP295 |
A | HIS333 |
A | HOH544 |
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 | SER310-PRO316 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31002765, ECO:0007744|PDB:6II7 |
Chain | Residue | Details |
A | HIS46 | |
A | HIS48 | |
A | HIS230 | |
A | ASP314 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A5KE01 |
Chain | Residue | Details |
A | ASP176 | |
A | GLU233 | |
A | HIS257 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:31002765, ECO:0007744|PDB:6II7 |
Chain | Residue | Details |
A | GLY205 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity for S-methyl-5'-thioadenosine => ECO:0000250|UniProtKB:A5KE01 |
Chain | Residue | Details |
A | ASP176 |