6F4L
Structure of quinolinate synthase with inhibitor-derived quinolinate
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 | MET83 |
A | CYS168 |
A | PRO169 |
A | GLU195 |
A | CYS254 |
A | NTM302 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue NTM A 302 |
Chain | Residue |
A | ASP35 |
A | SER36 |
A | TYR107 |
A | HIS193 |
A | GLU195 |
A | SER209 |
A | THR210 |
A | SF4301 |
A | HOH419 |
A | HIS19 |
A | TYR21 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | ASP69 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue NHE A 304 |
Chain | Residue |
A | PRO103 |
A | ASP135 |
A | SER136 |
A | ARG292 |
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 |