5KTP
Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound itaconate and Fe4S4 cluster
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 7 |
| Details | binding site for residue SF4 A 401 |
| Chain | Residue |
| A | CYS83 |
| A | MET85 |
| A | ASN111 |
| A | CYS170 |
| A | GLU198 |
| A | CYS256 |
| A | HOH757 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | GLN244 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue ITN A 403 |
| Chain | Residue |
| A | ASP37 |
| A | SER38 |
| A | TYR109 |
| A | ASN111 |
| A | THR125 |
| A | SER126 |
| A | HIS196 |
| A | GLU198 |
| A | SER212 |
| A | THR213 |
| A | HOH512 |
| A | HIS21 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NH4 A 404 |
| Chain | Residue |
| A | ASP137 |
| A | ARG239 |
| A | TYR242 |
| A | PRO243 |
| A | LYS245 |
| A | PHE247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:31390192, ECO:0000305|PubMed:15937336, ECO:0000305|PubMed:27224840, ECO:0000305|PubMed:27404889 |
| Chain | Residue | Details |
| A | HIS21 | |
| A | SER38 | |
| A | TYR109 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:27224840, ECO:0000269|PubMed:27404889, ECO:0000269|PubMed:31390192, ECO:0007744|PDB:4ZK6, ECO:0007744|PDB:5KTM, ECO:0007744|PDB:5KTN, ECO:0007744|PDB:5KTO, ECO:0007744|PDB:5KTP, ECO:0007744|PDB:5KTR, ECO:0007744|PDB:5KTS, ECO:0007744|PDB:5KTT |
| Chain | Residue | Details |
| A | CYS83 | |
| A | CYS170 | |
| A | CYS256 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00568, ECO:0000269|PubMed:31390192, ECO:0000305|PubMed:15937336, ECO:0000305|PubMed:27404889 |
| Chain | Residue | Details |
| A | SER126 | |
| A | HIS196 | |
| A | THR213 |
