4YSH
Crystal structure of glycine oxidase from Geobacillus kaustophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0043799 | molecular_function | glycine oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0071949 | molecular_function | FAD binding |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0043799 | molecular_function | glycine oxidase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue FAD A 401 |
| Chain | Residue |
| A | GLY11 |
| A | SER43 |
| A | ALA46 |
| A | ALA47 |
| A | GLY48 |
| A | MET49 |
| A | THR178 |
| A | VAL180 |
| A | ALA207 |
| A | SER208 |
| A | GLY209 |
| A | GLY13 |
| A | TRP211 |
| A | CYS232 |
| A | TYR253 |
| A | ARG309 |
| A | HIS334 |
| A | TYR335 |
| A | ARG336 |
| A | ASN337 |
| A | GLY338 |
| A | ILE339 |
| A | VAL14 |
| A | LEU340 |
| A | HOH501 |
| A | HOH503 |
| A | HOH506 |
| A | HOH507 |
| A | HOH518 |
| A | ILE15 |
| A | PHE33 |
| A | GLU34 |
| A | LYS35 |
| A | GLY41 |
| A | ALA42 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | ALA266 |
| A | THR267 |
| A | SER268 |
| A | ARG288 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GLY B 401 |
| Chain | Residue |
| B | GLY251 |
| B | TYR253 |
| B | ALA266 |
| B | ARG336 |
| B | GLY402 |
| B | HOH529 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GLY B 402 |
| Chain | Residue |
| B | GLU55 |
| B | TYR253 |
| B | ARG309 |
| B | ARG336 |
| B | GLY401 |
| B | FAD403 |
| site_id | AC5 |
| Number of Residues | 36 |
| Details | binding site for residue FAD B 403 |
| Chain | Residue |
| B | VAL10 |
| B | GLY11 |
| B | GLY13 |
| B | VAL14 |
| B | ILE15 |
| B | PHE33 |
| B | GLU34 |
| B | LYS35 |
| B | GLY41 |
| B | ALA42 |
| B | SER43 |
| B | ALA46 |
| B | ALA47 |
| B | GLY48 |
| B | MET49 |
| B | THR178 |
| B | GLU179 |
| B | VAL180 |
| B | SER208 |
| B | TRP211 |
| B | CYS232 |
| B | TYR253 |
| B | ARG309 |
| B | HIS334 |
| B | TYR335 |
| B | ARG336 |
| B | ASN337 |
| B | GLY338 |
| B | ILE339 |
| B | LEU340 |
| B | GLY402 |
| B | HOH510 |
| B | HOH518 |
| B | HOH537 |
| B | HOH545 |
| B | HOH550 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue IPA B 405 |
| Chain | Residue |
| B | ALA18 |
| B | GLU22 |
| B | LYS25 |
| B | PRO343 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 406 |
| Chain | Residue |
| B | ARG218 |
| B | ARG218 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 407 |
| Chain | Residue |
| B | THR267 |
| B | SER268 |
| B | ARG288 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|Ref.3 |
| Chain | Residue | Details |
| A | VAL14 | |
| B | GLU34 | |
| B | ALA42 | |
| B | ALA47 | |
| B | PHE181 | |
| B | PRO310 | |
| B | TYR335 | |
| B | ASN337 | |
| A | GLU34 | |
| A | ALA42 | |
| A | ALA47 | |
| A | PHE181 | |
| A | PRO310 | |
| A | TYR335 | |
| A | ASN337 | |
| B | VAL14 |
