5KTO
Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound quinolinate 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 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 | 6 |
| Details | binding site for residue SF4 A 401 |
| Chain | Residue |
| A | TYR23 |
| A | CYS83 |
| A | ALA84 |
| A | CYS170 |
| A | CYS256 |
| A | NTM402 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue NTM A 402 |
| Chain | Residue |
| A | SER38 |
| A | MET61 |
| A | TYR109 |
| A | HIS173 |
| A | HIS196 |
| A | GLU198 |
| A | MET259 |
| A | SF4401 |
| A | CL406 |
| A | HOH526 |
| A | HOH549 |
| A | HOH588 |
| A | HOH607 |
| A | HIS21 |
| A | TYR23 |
| A | ASP37 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EPE A 403 |
| Chain | Residue |
| A | LYS98 |
| A | PRO102 |
| A | ASN103 |
| A | PRO105 |
| A | ASP121 |
| A | ARG294 |
| A | HOH583 |
| A | HOH676 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | ILE17 |
| A | ARG44 |
| A | VAL48 |
| A | ASP49 |
| A | ALA50 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | LYS275 |
| A | TYR276 |
| A | LYS277 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | HIS196 |
| A | SER212 |
| A | THR213 |
| A | NTM402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31390192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15937336","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27224840","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27404889","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":"27224840","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27404889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31390192","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ZK6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KTT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00568","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31390192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15937336","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27404889","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
