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 |
B | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
B | 0009225 | biological_process | nucleotide-sugar metabolic process |
B | 0016829 | molecular_function | lyase 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 |
D | 0008460 | molecular_function | dTDP-glucose 4,6-dehydratase activity |
D | 0009225 | biological_process | nucleotide-sugar metabolic process |
D | 0016829 | molecular_function | lyase 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 | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | ASP125 | |
B | ASP125 | |
C | ASP125 | |
D | ASP125 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | GLU126 | |
A | TYR149 | |
B | GLU126 | |
B | TYR149 | |
C | GLU126 | |
C | TYR149 | |
D | GLU126 | |
D | TYR149 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | THR124 | |
B | THR124 | |
C | THR124 | |
D | THR124 |