1T6Y
Crystal structure of ADP, AMP, and FMN bound TM379
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003919 | molecular_function | FMN adenylyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006747 | biological_process | FAD biosynthetic process |
| A | 0006771 | biological_process | riboflavin metabolic process |
| A | 0008531 | molecular_function | riboflavin kinase activity |
| A | 0009231 | biological_process | riboflavin biosynthetic process |
| A | 0009398 | biological_process | FMN biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003919 | molecular_function | FMN adenylyltransferase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006747 | biological_process | FAD biosynthetic process |
| B | 0006771 | biological_process | riboflavin metabolic process |
| B | 0008531 | molecular_function | riboflavin kinase activity |
| B | 0009231 | biological_process | riboflavin biosynthetic process |
| B | 0009398 | biological_process | FMN biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP A 294 |
| Chain | Residue |
| A | HIS167 |
| A | LEU241 |
| A | TYR242 |
| A | HOH625 |
| A | PRO179 |
| A | THR180 |
| A | ALA181 |
| A | VAL232 |
| A | ILE234 |
| A | PHE237 |
| A | GLY239 |
| A | ASP240 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AMP A 295 |
| Chain | Residue |
| A | ILE5 |
| A | GLY6 |
| A | VAL7 |
| A | PHE8 |
| A | HIS12 |
| A | HIS15 |
| A | VAL18 |
| A | VAL98 |
| A | GLY99 |
| A | ASP101 |
| A | ASP127 |
| A | VAL128 |
| A | VAL135 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FMN A 296 |
| Chain | Residue |
| A | PHE178 |
| A | THR180 |
| A | VAL197 |
| A | VAL213 |
| A | ASN215 |
| A | LYS229 |
| A | GLU231 |
| A | ARG255 |
| A | GLU257 |
| A | LYS258 |
| A | LEU266 |
| A | ILE270 |
| B | GLU564 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ADP B 594 |
| Chain | Residue |
| B | PRO479 |
| B | THR480 |
| B | ALA481 |
| B | ASN482 |
| B | GLU531 |
| B | VAL532 |
| B | TYR533 |
| B | ILE534 |
| B | PHE537 |
| B | GLY539 |
| B | ASP540 |
| B | LEU541 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AMP B 595 |
| Chain | Residue |
| B | ILE305 |
| B | VAL307 |
| B | PHE308 |
| B | HIS315 |
| B | VAL318 |
| B | VAL398 |
| B | GLY399 |
| B | ARG400 |
| B | GLU426 |
| B | ASP427 |
| B | VAL428 |
| B | VAL435 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FMN B 596 |
| Chain | Residue |
| B | THR480 |
| B | VAL497 |
| B | VAL513 |
| B | ASN515 |
| B | PHE518 |
| B | LYS529 |
| B | GLU531 |
| B | ARG555 |
| B | GLU557 |
| B | LYS558 |
| B | LEU566 |
| B | ASP573 |
