1C3U
T. MARITIMA ADENYLOSUCCINATE LYASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| A | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| A | 0070626 | molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004018 | molecular_function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009152 | biological_process | purine ribonucleotide biosynthetic process |
| B | 0009168 | biological_process | purine ribonucleoside monophosphate biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0044208 | biological_process | 'de novo' AMP biosynthetic process |
| B | 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 | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 432 |
| Chain | Residue |
| A | SER306 |
| A | SER307 |
| A | ARG310 |
| A | HOH1025 |
| A | HOH1148 |
| B | ARG4 |
| B | ARG276 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 433 |
| Chain | Residue |
| A | HOH1126 |
| A | THR93 |
| A | SER94 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 432 |
| Chain | Residue |
| A | ARG4 |
| A | ARG276 |
| B | SER306 |
| B | SER307 |
| B | ARG310 |
| B | HOH2025 |
| B | HOH2148 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 433 |
| Chain | Residue |
| B | THR93 |
| B | SER94 |
| B | HOH2126 |
Functional Information from PROSITE/UniProt
| site_id | PS00163 |
| Number of Residues | 10 |
| Details | FUMARATE_LYASES Fumarate lyases signature. GSsaMpHKkN |
| Chain | Residue | Details |
| A | GLY261-ASN270 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10673438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P0AB89","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | THR140 | |
| A | HIS141 | |
| B | LYS268 | |
| B | GLU275 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1auw |
| Chain | Residue | Details |
| A | LYS268 | |
| A | GLU275 | |
| B | THR140 | |
| B | HIS141 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 80 |
| Chain | Residue | Details |
| A | HIS68 | electrostatic stabiliser |
| A | THR140 | electrostatic stabiliser |
| A | HIS141 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER263 | proton acceptor, proton donor |
| A | LYS268 | electrostatic stabiliser |
| A | GLU275 | activator, hydrogen bond acceptor, increase basicity |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 80 |
| Chain | Residue | Details |
| B | HIS68 | electrostatic stabiliser |
| B | THR140 | electrostatic stabiliser |
| B | HIS141 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | SER263 | proton acceptor, proton donor |
| B | LYS268 | electrostatic stabiliser |
| B | GLU275 | activator, hydrogen bond acceptor, increase basicity |
