6VLO
X-ray Structure of the R141 Sugar 4,6-dehydratase from Acanthamoeba polyphaga Minivirus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| A | 0009225 | biological_process | nucleotide-sugar metabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0050377 | molecular_function | UDP-glucose 4,6-dehydratase activity |
| B | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| B | 0009225 | biological_process | nucleotide-sugar metabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0050377 | molecular_function | UDP-glucose 4,6-dehydratase activity |
| C | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| C | 0009225 | biological_process | nucleotide-sugar metabolic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0050377 | molecular_function | UDP-glucose 4,6-dehydratase activity |
| D | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
| D | 0009225 | biological_process | nucleotide-sugar metabolic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0050377 | molecular_function | UDP-glucose 4,6-dehydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue TYD A 401 |
| Chain | Residue |
| A | ASN178 |
| A | VAL248 |
| A | ARG273 |
| A | ARG279 |
| A | HOH506 |
| A | HOH546 |
| A | HOH595 |
| A | HOH623 |
| A | GLU187 |
| A | LYS188 |
| A | LEU189 |
| A | LYS192 |
| A | HIS204 |
| A | GLN206 |
| A | SER211 |
| A | ARG213 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | binding site for residue NAD A 402 |
| Chain | Residue |
| A | GLY8 |
| A | LEU10 |
| A | GLY11 |
| A | PHE12 |
| A | ILE13 |
| A | ASP34 |
| A | ILE35 |
| A | GLY36 |
| A | ASP37 |
| A | CYS39 |
| A | ALA40 |
| A | GLY56 |
| A | ASP57 |
| A | ILE58 |
| A | PHE79 |
| A | ALA80 |
| A | ALA81 |
| A | SER83 |
| A | THR98 |
| A | MET122 |
| A | THR124 |
| A | LYS153 |
| A | HOH517 |
| A | HOH542 |
| A | HOH558 |
| A | HOH561 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue TYD B 401 |
| Chain | Residue |
| B | ASN178 |
| B | GLU187 |
| B | LYS188 |
| B | LEU189 |
| B | LYS192 |
| B | PHE193 |
| B | HIS204 |
| B | GLN206 |
| B | SER211 |
| B | ARG213 |
| B | VAL248 |
| B | ARG273 |
| B | ARG279 |
| B | HOH507 |
| B | HOH552 |
| B | HOH596 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | binding site for residue NAD B 402 |
| Chain | Residue |
| B | GLY8 |
| B | GLY11 |
| B | PHE12 |
| B | ILE13 |
| B | ASP34 |
| B | ILE35 |
| B | ASP37 |
| B | CYS39 |
| B | ALA40 |
| B | GLY56 |
| B | ASP57 |
| B | ILE58 |
| B | PHE79 |
| B | ALA80 |
| B | ALA81 |
| B | SER83 |
| B | THR98 |
| B | MET122 |
| B | SER123 |
| B | THR124 |
| B | LYS153 |
| B | CYS176 |
| B | ASN177 |
| B | ASN178 |
| B | VAL179 |
| B | HOH512 |
| B | HOH565 |
| B | HOH570 |
| B | HOH574 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue NI B 403 |
| Chain | Residue |
| B | HIS66 |
| B | HIS71 |
| D | HIS66 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue TYD C 401 |
| Chain | Residue |
| C | ARG213 |
| C | VAL248 |
| C | ARG273 |
| C | ARG279 |
| C | HOH523 |
| C | HOH541 |
| C | HOH552 |
| C | ASN178 |
| C | GLU187 |
| C | LYS188 |
| C | LEU189 |
| C | LYS192 |
| C | PHE193 |
| C | HIS204 |
| C | GLN206 |
| C | SER211 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for residue NAD C 402 |
| Chain | Residue |
| C | GLY8 |
| C | GLY11 |
| C | PHE12 |
| C | ILE13 |
| C | ASP34 |
| C | ILE35 |
| C | GLY36 |
| C | ASP37 |
| C | CYS39 |
| C | ALA40 |
| C | GLY56 |
| C | ASP57 |
| C | ILE58 |
| C | PHE79 |
| C | ALA80 |
| C | ALA81 |
| C | SER83 |
| C | MET122 |
| C | THR124 |
| C | LYS153 |
| C | HOH528 |
| C | HOH530 |
| C | HOH534 |
| C | HOH544 |
| C | HOH574 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue NI C 403 |
| Chain | Residue |
| A | HIS66 |
| A | HIS71 |
| C | HIS66 |
| C | GLU70 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue TYD D 401 |
| Chain | Residue |
| D | HIS84 |
| D | ASN178 |
| D | GLU187 |
| D | LYS188 |
| D | LEU189 |
| D | LYS192 |
| D | HIS204 |
| D | GLN206 |
| D | SER211 |
| D | ARG213 |
| D | VAL248 |
| D | ARG273 |
| D | ARG279 |
| D | HOH528 |
| D | HOH557 |
| site_id | AD1 |
| Number of Residues | 19 |
| Details | binding site for residue NAD D 402 |
| Chain | Residue |
| D | GLY8 |
| D | LEU10 |
| D | GLY11 |
| D | PHE12 |
| D | ILE13 |
| D | ASP34 |
| D | ILE35 |
| D | GLY36 |
| D | ASP37 |
| D | CYS39 |
| D | ALA40 |
| D | GLY56 |
| D | ASP57 |
| D | ILE58 |
| D | PHE79 |
| D | ALA80 |
| D | THR98 |
| D | HOH533 |
| D | HOH539 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
