5EYT
Crystal Structure of Adenylosuccinate Lyase from Schistosoma mansoni in complex with AMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006106 | biological_process | fumarate metabolic process |
| A | 0006166 | biological_process | purine ribonucleoside salvage |
| A | 0006167 | biological_process | AMP biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0032261 | biological_process | purine nucleotide salvage |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0044209 | biological_process | AMP salvage |
| A | 0051262 | biological_process | protein tetramerization |
| A | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue AMP A 1000 |
| Chain | Residue |
| A | ARG14 |
| A | LEU326 |
| A | SER329 |
| A | ALA330 |
| A | ARG333 |
| A | HOH1122 |
| A | HOH1152 |
| A | HOH1170 |
| A | TYR15 |
| A | ARG79 |
| A | HIS80 |
| A | ASP81 |
| A | SER106 |
| A | HIS153 |
| A | GLN236 |
| A | ARG298 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsaMpYKrN |
| Chain | Residue | Details |
| A | GLY283-ASN292 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28347672","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EYT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
