6F4D
Structure of the Y21F variant of quinolinate synthase in complex with PGH
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 aspartate |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue SF4 A 301 |
| Chain | Residue |
| A | PHE21 |
| A | CYS81 |
| A | ASN109 |
| A | CYS168 |
| A | GLU195 |
| A | CYS254 |
| A | PGH302 |
| A | HOH539 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue PGH A 302 |
| Chain | Residue |
| A | PHE21 |
| A | ASP35 |
| A | SER36 |
| A | ASN109 |
| A | SER124 |
| A | HIS171 |
| A | HIS193 |
| A | GLU195 |
| A | SER209 |
| A | THR210 |
| A | SF4301 |
| A | PO4303 |
| A | HOH409 |
| A | HOH413 |
| A | HOH446 |
| A | HOH539 |
| A | HIS19 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue PO4 A 303 |
| Chain | Residue |
| A | HIS19 |
| A | ASP35 |
| A | SER36 |
| A | SER124 |
| A | HIS193 |
| A | SER209 |
| A | THR210 |
| A | PGH302 |
| A | HOH413 |
| A | HOH446 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 304 |
| Chain | Residue |
| A | GLN38 |
| A | ARG41 |
| A | LYS215 |
| A | HOH482 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | ARG219 |
| A | LYS238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168, ECO:0000305|PubMed:30855610 |
| Chain | Residue | Details |
| A | HIS19 | |
| A | SER36 | |
| A | SER124 | |
| A | HIS193 | |
| A | THR210 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:24650327, ECO:0000269|PubMed:27545412, ECO:0000269|PubMed:29641168, ECO:0007744|PDB:4P3X, ECO:0007744|PDB:5F33, ECO:0007744|PDB:5F35, ECO:0007744|PDB:5F3D, ECO:0007744|PDB:5LQM, ECO:0007744|PDB:5LQS |
| Chain | Residue | Details |
| A | CYS81 | |
| A | CYS168 | |
| A | CYS254 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168 |
| Chain | Residue | Details |
| A | TYR107 |
