1TB3
Crystal Structure Analysis of Recombinant Rat Kidney Long-chain Hydroxy Acid Oxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0006629 | biological_process | lipid metabolic process |
| 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 | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005782 | cellular_component | peroxisomal matrix |
| B | 0006629 | biological_process | lipid metabolic process |
| 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 | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| C | 0005777 | cellular_component | peroxisome |
| C | 0005782 | cellular_component | peroxisomal matrix |
| C | 0006629 | biological_process | lipid metabolic process |
| 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 |
| D | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005782 | cellular_component | peroxisomal matrix |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0018924 | biological_process | mandelate metabolic process |
| D | 0019395 | biological_process | fatty acid oxidation |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| E | 0005777 | cellular_component | peroxisome |
| E | 0005782 | cellular_component | peroxisomal matrix |
| E | 0006629 | biological_process | lipid metabolic process |
| E | 0006631 | biological_process | fatty acid metabolic process |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0018924 | biological_process | mandelate metabolic process |
| E | 0019395 | biological_process | fatty acid oxidation |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| F | 0005777 | cellular_component | peroxisome |
| F | 0005782 | cellular_component | peroxisomal matrix |
| F | 0006629 | biological_process | lipid metabolic process |
| F | 0006631 | biological_process | fatty acid metabolic process |
| F | 0010181 | molecular_function | FMN binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0018924 | biological_process | mandelate metabolic process |
| F | 0019395 | biological_process | fatty acid oxidation |
| F | 0042802 | molecular_function | identical protein binding |
| G | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| G | 0005777 | cellular_component | peroxisome |
| G | 0005782 | cellular_component | peroxisomal matrix |
| G | 0006629 | biological_process | lipid metabolic process |
| G | 0006631 | biological_process | fatty acid metabolic process |
| G | 0010181 | molecular_function | FMN binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0018924 | biological_process | mandelate metabolic process |
| G | 0019395 | biological_process | fatty acid oxidation |
| G | 0042802 | molecular_function | identical protein binding |
| H | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| H | 0005777 | cellular_component | peroxisome |
| H | 0005782 | cellular_component | peroxisomal matrix |
| H | 0006629 | biological_process | lipid metabolic process |
| H | 0006631 | biological_process | fatty acid metabolic process |
| H | 0010181 | molecular_function | FMN binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0018924 | biological_process | mandelate metabolic process |
| H | 0019395 | biological_process | fatty acid oxidation |
| H | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 1401 |
| Chain | Residue |
| A | PHE23 |
| A | LYS223 |
| A | SER245 |
| A | HIS247 |
| A | ARG250 |
| A | ASP278 |
| A | GLY279 |
| A | GLY280 |
| A | ARG282 |
| A | GLY301 |
| A | ARG302 |
| A | ILE24 |
| A | LEU305 |
| A | ACY1402 |
| A | HOH1410 |
| A | HOH1415 |
| A | PRO76 |
| A | THR77 |
| A | ALA78 |
| A | SER105 |
| A | GLN127 |
| A | TYR129 |
| A | THR155 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN B 2401 |
| Chain | Residue |
| B | PHE23 |
| B | ILE24 |
| B | PRO76 |
| B | THR77 |
| B | ALA78 |
| B | SER105 |
| B | GLN127 |
| B | TYR129 |
| B | THR155 |
| B | LYS223 |
| B | SER245 |
| B | HIS247 |
| B | ARG250 |
| B | ASP278 |
| B | GLY279 |
| B | GLY280 |
| B | ARG282 |
| B | GLY301 |
| B | ARG302 |
| B | LEU305 |
| B | ACY2402 |
| B | HOH2411 |
| B | HOH2423 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN C 3401 |
| Chain | Residue |
| C | PHE23 |
| C | ILE24 |
| C | PRO76 |
| C | THR77 |
| C | ALA78 |
| C | SER105 |
| C | GLN127 |
| C | TYR129 |
| C | THR155 |
| C | LYS223 |
| C | SER245 |
| C | HIS247 |
| C | ARG250 |
| C | ASP278 |
| C | GLY279 |
| C | GLY280 |
| C | ARG282 |
| C | GLY301 |
| C | ARG302 |
| C | LEU305 |
| C | ACY3402 |
| C | HOH3405 |
| C | HOH3445 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN D 4401 |
| Chain | Residue |
| D | PHE23 |
| D | ILE24 |
| D | PRO76 |
| D | THR77 |
| D | ALA78 |
| D | SER105 |
| D | GLN127 |
| D | TYR129 |
| D | THR155 |
| D | LYS223 |
| D | SER245 |
| D | HIS247 |
| D | ARG250 |
| D | ASP278 |
| D | GLY279 |
| D | GLY280 |
| D | ARG282 |
| D | GLY301 |
| D | ARG302 |
| D | LEU305 |
| D | ACY4402 |
| D | HOH4421 |
| D | HOH4422 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN E 5401 |
| Chain | Residue |
| E | GLN127 |
| E | TYR129 |
| E | THR155 |
| E | LYS223 |
| E | SER245 |
| E | HIS247 |
| E | GLY248 |
| E | ARG250 |
| E | ASP278 |
| E | GLY279 |
| E | GLY280 |
| E | ARG282 |
| E | GLY301 |
| E | ARG302 |
| E | LEU305 |
| E | ACY5402 |
| E | HOH5425 |
| E | HOH5426 |
| E | PHE23 |
| E | ILE24 |
| E | SER75 |
| E | PRO76 |
| E | THR77 |
| E | ALA78 |
| E | SER105 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN F 6401 |
| Chain | Residue |
| F | PHE23 |
| F | ILE24 |
| F | PRO76 |
| F | THR77 |
| F | ALA78 |
| F | SER105 |
| F | GLN127 |
| F | TYR129 |
| F | THR155 |
| F | LYS223 |
| F | SER245 |
| F | HIS247 |
| F | ARG250 |
| F | ASP278 |
| F | GLY279 |
| F | GLY280 |
| F | ARG282 |
| F | GLY301 |
| F | ARG302 |
| F | LEU305 |
| F | ACY6402 |
| F | HOH6408 |
| F | HOH6421 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN G 7401 |
| Chain | Residue |
| G | PHE23 |
| G | ILE24 |
| G | PRO76 |
| G | THR77 |
| G | ALA78 |
| G | SER105 |
| G | GLN127 |
| G | TYR129 |
| G | THR155 |
| G | LYS223 |
| G | SER245 |
| G | HIS247 |
| G | ARG250 |
| G | ASP278 |
| G | GLY279 |
| G | GLY280 |
| G | ARG282 |
| G | GLY301 |
| G | ARG302 |
| G | LEU305 |
| G | ACY7402 |
| G | HOH7409 |
| G | HOH7427 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN H 8401 |
| Chain | Residue |
| H | PHE23 |
| H | ILE24 |
| H | PRO76 |
| H | THR77 |
| H | ALA78 |
| H | SER105 |
| H | GLN127 |
| H | TYR129 |
| H | THR155 |
| H | LYS223 |
| H | SER245 |
| H | HIS247 |
| H | ARG250 |
| H | ASP278 |
| H | GLY279 |
| H | GLY280 |
| H | ARG282 |
| H | GLY301 |
| H | ARG302 |
| H | LEU305 |
| H | ACY8402 |
| H | HOH8403 |
| H | HOH8441 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 1402 |
| Chain | Residue |
| A | TYR129 |
| A | ARG164 |
| A | HIS247 |
| A | ARG250 |
| A | FMN1401 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 2402 |
| Chain | Residue |
| B | TYR129 |
| B | ARG164 |
| B | HIS247 |
| B | ARG250 |
| B | FMN2401 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY C 3402 |
| Chain | Residue |
| C | TYR129 |
| C | ARG164 |
| C | HIS247 |
| C | FMN3401 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY D 4402 |
| Chain | Residue |
| D | TYR129 |
| D | ARG164 |
| D | HIS247 |
| D | FMN4401 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY E 5402 |
| Chain | Residue |
| E | TYR129 |
| E | ARG164 |
| E | HIS247 |
| E | ARG250 |
| E | FMN5401 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY F 6402 |
| Chain | Residue |
| F | TYR129 |
| F | ARG164 |
| F | HIS247 |
| F | ARG250 |
| F | FMN6401 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY G 7402 |
| Chain | Residue |
| G | TYR129 |
| G | ARG164 |
| G | HIS247 |
| G | FMN7401 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY H 8402 |
| Chain | Residue |
| H | TYR129 |
| H | ARG164 |
| H | HIS247 |
| H | FMN8401 |
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 | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15683236","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 88 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15683236","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22342614","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TB3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SGZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| A | TYR129 | |
| A | HIS247 | |
| A | ASP157 | |
| A | ARG250 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| B | TYR129 | |
| B | HIS247 | |
| B | ASP157 | |
| B | ARG250 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| C | TYR129 | |
| C | HIS247 | |
| C | ASP157 | |
| C | ARG250 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| D | TYR129 | |
| D | HIS247 | |
| D | ASP157 | |
| D | ARG250 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| E | TYR129 | |
| E | HIS247 | |
| E | ASP157 | |
| E | ARG250 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| F | TYR129 | |
| F | HIS247 | |
| F | ASP157 | |
| F | ARG250 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| G | TYR129 | |
| G | HIS247 | |
| G | ASP157 | |
| G | ARG250 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gox |
| Chain | Residue | Details |
| H | TYR129 | |
| H | HIS247 | |
| H | ASP157 | |
| H | ARG250 |
