1QDL
THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000162 | biological_process | L-tryptophan biosynthetic process |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004049 | molecular_function | anthranilate synthase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000162 | biological_process | L-tryptophan biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004049 | molecular_function | anthranilate synthase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00690 |
| Number of Residues | 10 |
| Details | DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. HsLVVDEVHR |
| Chain | Residue | Details |
| B | HIS136-ARG145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00897","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 192 |
| Details | Domain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile; for GATase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For GATase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00900","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11371633 |
| Chain | Residue | Details |
| A | HIS306 | |
| B | HIS175 | |
| B | GLU177 | |
| B | CYS84 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11371633 |
| Chain | Residue | Details |
| A | HIS306 | |
| B | HIS175 | |
| B | GLU177 | |
| B | CYS84 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 314 |
| Chain | Residue | Details |
| B | GLY56 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS84 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LEU85 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS175 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU177 | hydrogen bond acceptor, increase acidity, increase basicity |
