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 | 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 | 0016310 | biological_process | phosphorylation |
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 | 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 | 0016310 | biological_process | phosphorylation |
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 |