4XGV
Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase
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 |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| C | 0016740 | molecular_function | transferase activity |
| C | 0017013 | biological_process | protein flavinylation |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1990204 | cellular_component | oxidoreductase complex |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| D | 0016740 | molecular_function | transferase activity |
| D | 0017013 | biological_process | protein flavinylation |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1990204 | cellular_component | oxidoreductase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 501 |
| Chain | Residue |
| A | THR166 |
| A | ASP280 |
| A | ASP283 |
| A | THR284 |
| A | HOH698 |
| A | HOH721 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 502 |
| Chain | Residue |
| A | HOH685 |
| A | HOH746 |
| A | HOH750 |
| A | LYS134 |
| A | THR137 |
| A | HOH652 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | GLY237 |
| A | SER238 |
| A | TYR239 |
| A | ARG240 |
| A | SER251 |
| A | HIS252 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | PRO77 |
| A | TYR152 |
| A | HOH640 |
| A | HOH683 |
| A | HOH715 |
| D | TRP78 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ASP174 |
| A | ALA177 |
| A | ARG178 |
| A | THR275 |
| A | HOH612 |
| A | HOH641 |
| A | HOH647 |
| A | HOH737 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | GLN49 |
| A | HIS175 |
| A | LEU179 |
| A | GLN182 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 507 |
| Chain | Residue |
| A | ASP99 |
| A | ALA101 |
| A | ASP255 |
| A | GLN257 |
| A | LEU289 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 501 |
| Chain | Residue |
| B | THR166 |
| B | ASP280 |
| B | ASP283 |
| B | THR284 |
| B | HOH712 |
| B | HOH759 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | HIS231 |
| B | ILE272 |
| B | ALA273 |
| B | PRO274 |
| B | GLY302 |
| B | ALA304 |
| B | PHE326 |
| D | GLU181 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | ARG178 |
| B | HOH648 |
| D | PRO274 |
| D | HOH621 |
| D | HOH642 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 504 |
| Chain | Residue |
| B | LEU289 |
| B | GLY290 |
| B | PRO291 |
| B | GLU292 |
| B | LYS293 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | GLY194 |
| B | LEU196 |
| B | THR235 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | HIS175 |
| B | ARG178 |
| B | HOH615 |
| B | HOH667 |
| B | HOH750 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 501 |
| Chain | Residue |
| C | THR166 |
| C | ASP280 |
| C | ASP283 |
| C | THR284 |
| C | HOH703 |
| C | HOH748 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| C | LYS134 |
| C | THR137 |
| C | HOH712 |
| C | HOH734 |
| C | HOH755 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| A | PRO274 |
| A | HOH617 |
| A | HOH637 |
| A | HOH662 |
| C | ARG178 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 501 |
| Chain | Residue |
| D | THR166 |
| D | ASP280 |
| D | ASP283 |
| D | THR284 |
| D | HOH724 |
| D | HOH760 |
| site_id | AD9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | THR275 |
| D | HOH629 |
| D | HOH661 |
| D | HOH729 |
| B | HOH657 |
| D | ASP174 |
| D | ALA177 |
| D | ARG178 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| D | TYR171 |
| D | ASP174 |
| D | HIS175 |
| D | ARG178 |
| D | HOH615 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 504 |
| Chain | Residue |
| D | MET23 |
| D | ASP54 |
| D | LEU57 |
| D | SER58 |
| D | SER165 |
| D | HOH663 |
| D | HOH733 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P41780","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| 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 |
