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 | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976 |
Chain | Residue | Details |
A | PRO203 | |
B | PRO203 | |
C | PRO203 | |
D | PRO203 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8R123 |
Chain | Residue | Details |
A | GLN475 | |
B | GLN475 | |
C | GLN475 | |
D | GLN475 |