1QDL
THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000162 | biological_process | tryptophan biosynthetic process |
A | 0004049 | molecular_function | anthranilate synthase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000162 | biological_process | tryptophan biosynthetic process |
B | 0004049 | molecular_function | anthranilate synthase activity |
B | 0006541 | biological_process | glutamine metabolic process |
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 | 1 |
Details | ACT_SITE: Nucleophile; for GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605 |
Chain | Residue | Details |
B | CYS84 | |
A | PRO207 | |
A | GLY242 | |
A | GLU269 | |
A | TYR357 | |
A | ARG377 | |
A | GLY391 | |
A | GLY393 | |
A | GLU406 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605 |
Chain | Residue | Details |
B | HIS175 | |
B | GLU177 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00900 |
Chain | Residue | Details |
B | GLY54 | |
B | GLN88 | |
B | SER137 |
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 |