3SGZ
High resolution crystal structure of rat long chain hydroxy acid oxidase in complex with the inhibitor 4-carboxy-5-[(4-chiorophenyl)sulfanyl]-1, 2, 3-thiadiazole.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001561 | biological_process | fatty acid alpha-oxidation |
| A | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018924 | biological_process | mandelate metabolic process |
| A | 0019395 | biological_process | fatty acid oxidation |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0001561 | biological_process | fatty acid alpha-oxidation |
| B | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005782 | cellular_component | peroxisomal matrix |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018924 | biological_process | mandelate metabolic process |
| B | 0019395 | biological_process | fatty acid oxidation |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0001561 | biological_process | fatty acid alpha-oxidation |
| C | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005782 | cellular_component | peroxisomal matrix |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018924 | biological_process | mandelate metabolic process |
| C | 0019395 | biological_process | fatty acid oxidation |
| C | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN A 401 |
| Chain | Residue |
| A | PHE23 |
| A | THR155 |
| A | LYS223 |
| A | SER245 |
| A | HIS247 |
| A | GLY248 |
| A | ARG250 |
| A | ASP278 |
| A | GLY279 |
| A | GLY280 |
| A | ARG282 |
| A | ILE24 |
| A | GLY301 |
| A | ARG302 |
| A | PRO303 |
| A | LEU305 |
| A | HO6402 |
| A | HOH503 |
| A | HOH504 |
| A | SER75 |
| A | PRO76 |
| A | THR77 |
| A | ALA78 |
| A | SER105 |
| A | GLN127 |
| A | TYR129 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HO6 A 402 |
| Chain | Residue |
| A | PHE23 |
| A | PHE79 |
| A | TYR107 |
| A | TYR129 |
| A | ARG164 |
| A | LEU198 |
| A | HIS247 |
| A | ARG250 |
| A | FMN401 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN B 401 |
| Chain | Residue |
| B | PHE23 |
| B | ILE24 |
| B | SER75 |
| B | PRO76 |
| B | THR77 |
| B | ALA78 |
| B | SER105 |
| B | GLN127 |
| B | TYR129 |
| B | THR155 |
| B | LYS223 |
| B | SER245 |
| B | HIS247 |
| B | GLY248 |
| B | ARG250 |
| B | ASP278 |
| B | GLY279 |
| B | GLY280 |
| B | ARG282 |
| B | GLY301 |
| B | ARG302 |
| B | PRO303 |
| B | LEU305 |
| B | HO6402 |
| B | HOH503 |
| B | HOH509 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HO6 B 402 |
| Chain | Residue |
| B | PHE23 |
| B | PHE79 |
| B | TYR107 |
| B | TYR129 |
| B | LEU161 |
| B | ARG164 |
| B | LEU198 |
| B | PHE199 |
| B | HIS247 |
| B | ARG250 |
| B | FMN401 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN C 401 |
| Chain | Residue |
| C | PHE23 |
| C | ILE24 |
| C | SER75 |
| C | PRO76 |
| C | THR77 |
| C | ALA78 |
| C | SER105 |
| C | GLN127 |
| C | TYR129 |
| C | THR155 |
| C | LYS223 |
| C | SER245 |
| C | HIS247 |
| C | GLY248 |
| C | ARG250 |
| C | ASP278 |
| C | GLY279 |
| C | GLY280 |
| C | ARG282 |
| C | GLY301 |
| C | ARG302 |
| C | PRO303 |
| C | LEU305 |
| C | HO6402 |
| C | HOH1002 |
| C | HOH1006 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE HO6 C 402 |
| Chain | Residue |
| C | PHE79 |
| C | TYR107 |
| C | TYR129 |
| C | ARG164 |
| C | LEU198 |
| C | HIS247 |
| C | ARG250 |
| C | FMN401 |
| C | PHE23 |
Functional Information from PROSITE/UniProt
| site_id | PS00557 |
| Number of Residues | 7 |
| Details | FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ |
| Chain | Residue | Details |
| A | SER245-GLN251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000305|PubMed:15683236 |
| Chain | Residue | Details |
| A | HIS247 | |
| B | HIS247 | |
| C | HIS247 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15683236, ECO:0000269|PubMed:22342614, ECO:0007744|PDB:1TB3, ECO:0007744|PDB:3SGZ |
| Chain | Residue | Details |
| A | PRO76 | |
| B | GLN127 | |
| B | THR155 | |
| B | LYS223 | |
| B | ASP278 | |
| B | GLY301 | |
| C | PRO76 | |
| C | SER105 | |
| C | GLN127 | |
| C | THR155 | |
| C | LYS223 | |
| A | SER105 | |
| C | ASP278 | |
| C | GLY301 | |
| A | GLN127 | |
| A | THR155 | |
| A | LYS223 | |
| A | ASP278 | |
| A | GLY301 | |
| B | PRO76 | |
| B | SER105 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683 |
| Chain | Residue | Details |
| A | TYR129 | |
| A | ARG164 | |
| A | ARG250 | |
| B | TYR129 | |
| B | ARG164 | |
| B | ARG250 | |
| C | TYR129 | |
| C | ARG164 | |
| C | ARG250 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| A | SER132 | |
| B | SER132 | |
| C | SER132 |
