8RON
Crystal structure of human FAD synthase, isoform 2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003919 | molecular_function | FMN adenylyltransferase activity |
| A | 0006747 | biological_process | FAD biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003919 | molecular_function | FMN adenylyltransferase activity |
| B | 0006747 | biological_process | FAD biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003919 | molecular_function | FMN adenylyltransferase activity |
| C | 0006747 | biological_process | FAD biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003919 | molecular_function | FMN adenylyltransferase activity |
| D | 0006747 | biological_process | FAD biosynthetic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 976 |
| Details | Region: {"description":"FAD diphosphatase","evidences":[{"source":"PubMed","id":"38688286","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38688286","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8ROM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q6FNA9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q8R123","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
