6G74
Structure of the Y21F variant of quinolinate synthase in complex with phthalate
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 |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008987 | molecular_function | quinolinate synthetase A activity |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0019805 | biological_process | quinolinate biosynthetic process |
| B | 0034628 | biological_process | 'de novo' NAD biosynthetic process from aspartate |
| B | 0046872 | molecular_function | metal ion binding |
| B | 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 | GLU195 |
| A | CYS254 |
| A | PHT302 |
| A | HOH580 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue PHT A 302 |
| Chain | Residue |
| A | ASP35 |
| A | SER36 |
| A | ASN109 |
| A | SER124 |
| A | HIS193 |
| A | GLU195 |
| A | THR210 |
| A | SF4301 |
| A | HOH404 |
| A | HOH554 |
| A | HOH566 |
| A | HOH580 |
| A | HIS19 |
| A | PHE21 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SF4 B 301 |
| Chain | Residue |
| B | CYS81 |
| B | ASN109 |
| B | CYS168 |
| B | VAL170 |
| B | CYS254 |
| B | PHT302 |
| B | HOH575 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue PHT B 302 |
| Chain | Residue |
| B | HIS19 |
| B | PHE21 |
| B | ASP35 |
| B | SER36 |
| B | ASN109 |
| B | SER124 |
| B | HIS193 |
| B | GLU195 |
| B | THR210 |
| B | SF4301 |
| B | HOH408 |
| B | HOH519 |
| B | HOH541 |
| B | HOH571 |
| B | HOH575 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| 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 | |
| B | THR210 | |
| A | SER36 | |
| A | SER124 | |
| A | HIS193 | |
| A | THR210 | |
| B | HIS19 | |
| B | SER36 | |
| B | SER124 | |
| B | HIS193 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| 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 | |
| B | CYS81 | |
| B | CYS168 | |
| B | CYS254 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000305|PubMed:27545412, ECO:0000305|PubMed:29641168 |
| Chain | Residue | Details |
| A | TYR107 | |
| B | TYR107 |
