6F48
Structure of quinolinate synthase with reaction intermediates X and Y
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008987 | molecular_function | quinolinate synthetase A activity |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0019805 | biological_process | quinolinate biosynthetic process |
| A | 0034628 | biological_process | 'de novo' NAD+ biosynthetic process from L-aspartate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 A 301 |
| Chain | Residue |
| A | CYS81 |
| A | ASN109 |
| A | CYS168 |
| A | CYS254 |
| A | XQB302 |
| A | YQA305 |
| A | HOH630 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue XQB A 302 |
| Chain | Residue |
| A | ASP35 |
| A | SER36 |
| A | MET59 |
| A | TYR107 |
| A | VAL108 |
| A | ASN109 |
| A | SER124 |
| A | HIS171 |
| A | HIS193 |
| A | GLU195 |
| A | THR210 |
| A | SF4301 |
| A | YQA305 |
| A | HOH470 |
| A | HOH482 |
| A | HOH504 |
| A | HOH630 |
| A | HOH652 |
| A | HIS19 |
| A | PHE21 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | ARG96 |
| A | PRO100 |
| A | ALA102 |
| A | ASP119 |
| A | HOH493 |
| A | HOH566 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | ASN67 |
| A | ASP69 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue YQA A 305 |
| Chain | Residue |
| A | HIS19 |
| A | PHE21 |
| A | ASP35 |
| A | SER36 |
| A | MET59 |
| A | ASN109 |
| A | SER124 |
| A | HIS193 |
| A | SER209 |
| A | THR210 |
| A | SF4301 |
| A | XQB302 |
| A | HOH422 |
| A | HOH470 |
| A | HOH482 |
| A | HOH504 |
| A | HOH630 |
| A | HOH652 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | ASP135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27545412","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29641168","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30855610","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24650327","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27545412","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29641168","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4P3X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F33","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F3D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LQM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LQS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27545412","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29641168","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
