3R3S
Structure of the YghA Oxidoreductase from Salmonella enterica
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAD A 300 |
Chain | Residue |
A | ASP58 |
A | LEU109 |
A | VAL135 |
A | ALA136 |
A | GLY137 |
A | VAL159 |
A | SER185 |
A | SER186 |
A | TYR199 |
A | LYS203 |
A | PRO229 |
A | SER59 |
A | GLY230 |
A | PRO231 |
A | ILE232 |
A | THR234 |
A | LEU236 |
A | GLN237 |
A | FMT295 |
A | MG296 |
A | HOH297 |
A | HOH301 |
A | GLY60 |
A | HOH305 |
A | HOH319 |
A | HOH331 |
A | HOH439 |
A | HOH1604 |
A | ILE61 |
A | TYR80 |
A | LEU81 |
A | GLU84 |
A | GLY107 |
A | ASP108 |
site_id | AC2 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAD B 300 |
Chain | Residue |
B | ASP58 |
B | SER59 |
B | GLY60 |
B | ILE61 |
B | TYR80 |
B | LEU81 |
B | GLU84 |
B | GLY107 |
B | ASP108 |
B | LEU109 |
B | VAL135 |
B | ALA136 |
B | GLY137 |
B | VAL159 |
B | SER185 |
B | SER186 |
B | TYR199 |
B | LYS203 |
B | PRO229 |
B | GLY230 |
B | PRO231 |
B | ILE232 |
B | THR234 |
B | LEU236 |
B | GLN237 |
B | FMT295 |
B | MG296 |
B | HOH299 |
B | HOH315 |
B | HOH317 |
B | HOH336 |
B | HOH344 |
B | HOH350 |
site_id | AC3 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAD C 300 |
Chain | Residue |
C | HOH323 |
C | HOH1570 |
C | ASP58 |
C | SER59 |
C | GLY60 |
C | ILE61 |
C | TYR80 |
C | LEU81 |
C | GLU84 |
C | GLY107 |
C | ASP108 |
C | LEU109 |
C | VAL135 |
C | ALA136 |
C | GLY137 |
C | VAL159 |
C | SER185 |
C | SER186 |
C | TYR199 |
C | LYS203 |
C | PRO229 |
C | GLY230 |
C | PRO231 |
C | ILE232 |
C | THR234 |
C | LEU236 |
C | GLN237 |
C | FMT295 |
C | MG296 |
C | HOH297 |
C | HOH301 |
C | HOH311 |
C | HOH316 |
C | HOH318 |
site_id | AC4 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE NAD D 300 |
Chain | Residue |
D | ASP58 |
D | SER59 |
D | GLY60 |
D | ILE61 |
D | TYR80 |
D | LEU81 |
D | GLU84 |
D | GLY107 |
D | ASP108 |
D | LEU109 |
D | VAL135 |
D | ALA136 |
D | GLY137 |
D | VAL159 |
D | SER185 |
D | SER186 |
D | TYR199 |
D | LYS203 |
D | PRO229 |
D | GLY230 |
D | PRO231 |
D | ILE232 |
D | THR234 |
D | LEU236 |
D | GLN237 |
D | FMT295 |
D | MG296 |
D | HOH297 |
D | HOH299 |
D | HOH313 |
D | HOH320 |
D | HOH337 |
D | HOH370 |
D | HOH888 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 295 |
Chain | Residue |
A | GLN139 |
A | SER186 |
A | TYR199 |
A | NAD300 |
A | HOH405 |
A | HOH439 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT B 295 |
Chain | Residue |
B | GLN139 |
B | SER186 |
B | TYR199 |
B | NAD300 |
B | HOH344 |
B | HOH675 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT C 295 |
Chain | Residue |
C | GLN139 |
C | SER186 |
C | TYR199 |
C | NAD300 |
C | HOH301 |
C | HOH399 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT D 295 |
Chain | Residue |
D | SER186 |
D | GLN188 |
D | TYR199 |
D | NAD300 |
D | HOH370 |
D | HOH393 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 296 |
Chain | Residue |
A | ASP58 |
A | SER59 |
A | GLU84 |
A | HOH297 |
A | HOH298 |
A | NAD300 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 296 |
Chain | Residue |
B | ASP58 |
B | SER59 |
B | GLU84 |
B | HOH299 |
B | NAD300 |
B | HOH301 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 296 |
Chain | Residue |
C | ASP58 |
C | SER59 |
C | GLU84 |
C | HOH297 |
C | NAD300 |
C | HOH303 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 296 |
Chain | Residue |
D | ASP58 |
D | SER59 |
D | GLU84 |
D | HOH297 |
D | HOH298 |
D | NAD300 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 297 |
Chain | Residue |
B | GLN90 |
B | HOH569 |
B | HOH769 |
B | HOH834 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SiqayqpsphLldYAATKAAIlNYSrGLA |
Chain | Residue | Details |
A | SER186-ALA214 |