4XGX
Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, Y60N mutant, ADP-inhibited
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017013 | biological_process | protein flavinylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990204 | cellular_component | oxidoreductase complex |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017013 | biological_process | protein flavinylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | THR166 |
| A | ASP280 |
| A | THR284 |
| A | HOH589 |
| A | HOH617 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | GLU169 |
| A | TYR239 |
| A | ARG240 |
| A | ADP403 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue ADP A 403 |
| Chain | Residue |
| A | ALA101 |
| A | ASP103 |
| A | VAL106 |
| A | ASP163 |
| A | THR166 |
| A | SER238 |
| A | TYR239 |
| A | ARG240 |
| A | HIS252 |
| A | ILE254 |
| A | MG402 |
| A | HOH522 |
| A | HOH544 |
| A | HOH589 |
| A | HOH591 |
| A | HOH614 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue NO3 A 404 |
| Chain | Residue |
| A | ARG93 |
| A | ILE94 |
| A | LYS97 |
| A | GLU278 |
| A | TRP282 |
| A | HOH510 |
| A | HOH521 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue NO3 A 405 |
| Chain | Residue |
| A | GLN147 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue NO3 A 406 |
| Chain | Residue |
| A | HIS231 |
| A | ILE272 |
| A | ALA273 |
| A | PRO274 |
| A | PHE326 |
| A | HOH561 |
| B | ARG178 |
| B | GLU181 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 A 407 |
| Chain | Residue |
| A | THR89 |
| A | ARG93 |
| A | NO3408 |
| B | ASP86 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue NO3 A 408 |
| Chain | Residue |
| A | ASP86 |
| A | NO3407 |
| B | ASP86 |
| B | THR89 |
| B | THR90 |
| B | ARG93 |
| B | HOH534 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | ASP227 |
| A | ILE228 |
| A | ASN229 |
| A | HIS231 |
| B | SER186 |
| B | ARG199 |
| B | GLY200 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | ASP174 |
| A | ARG178 |
| A | GLU181 |
| A | HOH545 |
| A | HOH601 |
| B | PRO274 |
| B | EDO409 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | THR166 |
| B | ASP280 |
| B | THR284 |
| B | HOH647 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | GLU169 |
| B | TYR239 |
| B | ADP403 |
| site_id | AD4 |
| Number of Residues | 19 |
| Details | binding site for residue ADP B 403 |
| Chain | Residue |
| B | ALA101 |
| B | ASP103 |
| B | VAL106 |
| B | ASP163 |
| B | SER165 |
| B | THR166 |
| B | GLY237 |
| B | SER238 |
| B | TYR239 |
| B | ARG240 |
| B | HIS252 |
| B | VAL253 |
| B | ILE254 |
| B | MG402 |
| B | NO3405 |
| B | HOH502 |
| B | HOH519 |
| B | HOH540 |
| B | HOH568 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 B 404 |
| Chain | Residue |
| B | PRO77 |
| B | GLN147 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue NO3 B 405 |
| Chain | Residue |
| B | ADP403 |
| B | HOH647 |
| B | SER236 |
| B | GLY237 |
| B | VAL253 |
| B | ASP283 |
| B | THR284 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue NO3 B 406 |
| Chain | Residue |
| A | GLU82 |
| B | ARG93 |
| B | LYS97 |
| B | GLU278 |
| B | TRP282 |
| B | HOH574 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 B 407 |
| Chain | Residue |
| B | ASP174 |
| B | GLU181 |
| B | EDO408 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | ASP174 |
| B | HIS175 |
| B | NO3407 |
| B | HOH573 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| A | ARG199 |
| A | GLY230 |
| A | EDO410 |
| B | GLY230 |
| B | HIS231 |
| B | HOH571 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P41780","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of a thiamine biosynthesis lipoprotein ApbE.","authoringGroup":["Northeast structural genomics consortium (NESG)"]}},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
