1RYI
STRUCTURE OF GLYCINE OXIDASE WITH BOUND INHIBITOR GLYCOLATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0009635 | biological_process | response to herbicide |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0043799 | molecular_function | glycine oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0071949 | molecular_function | FAD binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0009635 | biological_process | response to herbicide |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0043799 | molecular_function | glycine oxidase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0071949 | molecular_function | FAD binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0009228 | biological_process | thiamine biosynthetic process |
| C | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| C | 0009635 | biological_process | response to herbicide |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0043799 | molecular_function | glycine oxidase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0009228 | biological_process | thiamine biosynthetic process |
| D | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| D | 0009635 | biological_process | response to herbicide |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0043799 | molecular_function | glycine oxidase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 9100 |
| Chain | Residue |
| A | GLY11 |
| A | ALA46 |
| A | ALA47 |
| A | GLY48 |
| A | MET49 |
| A | VAL174 |
| A | SER202 |
| A | GLY203 |
| A | TRP205 |
| A | PHE209 |
| A | CYS226 |
| A | GLY13 |
| A | TYR246 |
| A | GLY300 |
| A | HIS327 |
| A | PHE328 |
| A | ARG329 |
| A | ASN330 |
| A | GLY331 |
| A | ILE332 |
| A | LEU333 |
| A | GOA9110 |
| A | ILE14 |
| A | HOH9111 |
| A | HOH9112 |
| A | HOH9113 |
| A | HOH9114 |
| A | HOH9115 |
| A | HOH9121 |
| A | HOH9250 |
| A | ILE15 |
| A | PHE33 |
| A | GLU34 |
| A | SER35 |
| A | THR42 |
| A | THR43 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 9200 |
| Chain | Residue |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | ILE14 |
| B | ILE15 |
| B | PHE33 |
| B | GLU34 |
| B | SER35 |
| B | ARG41 |
| B | THR42 |
| B | THR43 |
| B | ALA46 |
| B | ALA47 |
| B | GLY48 |
| B | MET49 |
| B | VAL174 |
| B | SER202 |
| B | TRP205 |
| B | PHE209 |
| B | CYS226 |
| B | TYR246 |
| B | GLY300 |
| B | ARG302 |
| B | HIS327 |
| B | PHE328 |
| B | ARG329 |
| B | ASN330 |
| B | GLY331 |
| B | ILE332 |
| B | LEU333 |
| B | GOA9210 |
| B | HOH9211 |
| B | HOH9212 |
| B | HOH9213 |
| B | HOH9214 |
| B | HOH9215 |
| B | HOH9218 |
| B | HOH9237 |
| B | HOH9299 |
| B | HOH9450 |
| site_id | AC3 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE FAD C 9300 |
| Chain | Residue |
| C | HIS327 |
| C | PHE328 |
| C | ARG329 |
| C | ASN330 |
| C | GLY331 |
| C | ILE332 |
| C | LEU333 |
| C | GOA9310 |
| C | HOH9312 |
| C | HOH9313 |
| C | HOH9314 |
| C | HOH9315 |
| C | HOH9316 |
| C | HOH9326 |
| C | HOH9335 |
| C | HOH9399 |
| C | GLY11 |
| C | GLY13 |
| C | ILE14 |
| C | ILE15 |
| C | PHE33 |
| C | GLU34 |
| C | SER35 |
| C | ARG41 |
| C | THR42 |
| C | THR43 |
| C | ALA46 |
| C | ALA47 |
| C | GLY48 |
| C | MET49 |
| C | PRO173 |
| C | VAL174 |
| C | SER202 |
| C | TRP205 |
| C | PHE209 |
| C | CYS226 |
| C | TYR246 |
| C | GLY300 |
| C | ARG302 |
| site_id | AC4 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD D 9400 |
| Chain | Residue |
| D | ILE10 |
| D | GLY11 |
| D | GLY13 |
| D | ILE14 |
| D | ILE15 |
| D | PHE33 |
| D | GLU34 |
| D | SER35 |
| D | ARG41 |
| D | THR42 |
| D | THR43 |
| D | ALA46 |
| D | ALA47 |
| D | GLY48 |
| D | MET49 |
| D | PRO173 |
| D | VAL174 |
| D | SER202 |
| D | GLY203 |
| D | TRP205 |
| D | PHE209 |
| D | CYS226 |
| D | TYR246 |
| D | GLY300 |
| D | ARG302 |
| D | HIS327 |
| D | PHE328 |
| D | ARG329 |
| D | ASN330 |
| D | GLY331 |
| D | ILE332 |
| D | LEU333 |
| D | GOA9410 |
| D | HOH9411 |
| D | HOH9413 |
| D | HOH9415 |
| D | HOH9418 |
| D | HOH9422 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOA A 9110 |
| Chain | Residue |
| A | TYR246 |
| A | ALA259 |
| A | ARG302 |
| A | ARG329 |
| A | FAD9100 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOA B 9210 |
| Chain | Residue |
| B | TYR246 |
| B | ALA259 |
| B | ARG302 |
| B | ARG329 |
| B | FAD9200 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOA C 9310 |
| Chain | Residue |
| C | TYR246 |
| C | ALA259 |
| C | ARG302 |
| C | ARG329 |
| C | FAD9300 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOA D 9410 |
| Chain | Residue |
| D | TYR246 |
| D | ALA259 |
| D | ARG302 |
| D | ARG329 |
| D | FAD9400 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12627963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15105420","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19864430","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12627963","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1c0k |
| Chain | Residue | Details |
| A | ARG329 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1c0k |
| Chain | Residue | Details |
| B | ARG329 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1c0k |
| Chain | Residue | Details |
| C | ARG329 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1c0k |
| Chain | Residue | Details |
| D | ARG329 |
