3SGL
The crystal structure of MnmC from Yersinia pestis bound with FAD and SAM
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002097 | biological_process | tRNA wobble base modification |
A | 0002098 | biological_process | tRNA wobble uridine modification |
A | 0004808 | molecular_function | tRNA (5-methylaminomethyl-2-thiouridylate)(34)-methyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008033 | biological_process | tRNA processing |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008757 | molecular_function | S-adenosylmethionine-dependent methyltransferase activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016645 | molecular_function | oxidoreductase activity, acting on the CH-NH group of donors |
A | 0032259 | biological_process | methylation |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE FAD A 690 |
Chain | Residue |
A | ILE270 |
A | GLY302 |
A | ALA303 |
A | SER304 |
A | ASN306 |
A | ALA310 |
A | HIS433 |
A | GLU434 |
A | LEU435 |
A | ALA464 |
A | THR465 |
A | GLY271 |
A | GLY466 |
A | GLY485 |
A | VAL487 |
A | TYR508 |
A | GLY569 |
A | LEU627 |
A | GLY628 |
A | SER629 |
A | ARG630 |
A | GLY631 |
A | GLY272 |
A | LEU632 |
A | CL691 |
A | HOH715 |
A | HOH722 |
A | HOH735 |
A | HOH737 |
A | HOH752 |
A | HOH767 |
A | HOH774 |
A | GLY273 |
A | ILE274 |
A | VAL275 |
A | TYR293 |
A | ALA295 |
A | ASP296 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 691 |
Chain | Residue |
A | ASN306 |
A | GLY309 |
A | PRO411 |
A | FAD690 |
A | HOH778 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAM A 692 |
Chain | Residue |
A | GLU64 |
A | GLY66 |
A | PHE67 |
A | GLY68 |
A | THR69 |
A | GLY70 |
A | LEU71 |
A | ASN72 |
A | GLU101 |
A | LYS102 |
A | TYR103 |
A | GLY155 |
A | ASP156 |
A | VAL157 |
A | ASP178 |
A | GLY179 |
A | PHE180 |