2W0U
CRYSTAL STRUCTURE OF HUMAN GLYCOLATE OXIDASE IN COMPLEX WITH THE INHIBITOR 5-[(4-CHLOROPHENYL)SULFANYL]- 1,2,3-THIADIAZOLE-4-CARBOXYLATE.
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 | 0005829 | cellular_component | cytosol |
| A | 0006545 | biological_process | glycine biosynthetic process |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046296 | biological_process | glycolate catabolic process |
| A | 0047969 | molecular_function | glyoxylate oxidase activity |
| 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 | 0005829 | cellular_component | cytosol |
| B | 0006545 | biological_process | glycine biosynthetic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046296 | biological_process | glycolate catabolic process |
| B | 0047969 | molecular_function | glyoxylate oxidase activity |
| 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 | 0005829 | cellular_component | cytosol |
| C | 0006545 | biological_process | glycine biosynthetic process |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| C | 0046296 | biological_process | glycolate catabolic process |
| C | 0047969 | molecular_function | glyoxylate oxidase activity |
| D | 0001561 | biological_process | fatty acid alpha-oxidation |
| D | 0003973 | molecular_function | (S)-2-hydroxy-acid oxidase activity |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005782 | cellular_component | peroxisomal matrix |
| D | 0005829 | cellular_component | cytosol |
| D | 0006545 | biological_process | glycine biosynthetic process |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| D | 0046296 | biological_process | glycolate catabolic process |
| D | 0047969 | molecular_function | glyoxylate oxidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 1365 |
| Chain | Residue |
| A | TYR27 |
| A | LYS236 |
| A | SER258 |
| A | HIS260 |
| A | GLY261 |
| A | ARG263 |
| A | ASP291 |
| A | GLY292 |
| A | GLY293 |
| A | ARG295 |
| A | VAL313 |
| A | ALA79 |
| A | GLY314 |
| A | ARG315 |
| A | C7C1364 |
| A | THR80 |
| A | ALA81 |
| A | SER108 |
| A | SER109 |
| A | GLN130 |
| A | TYR132 |
| A | THR158 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN B 1365 |
| Chain | Residue |
| B | TYR27 |
| B | ALA79 |
| B | THR80 |
| B | ALA81 |
| B | SER108 |
| B | SER109 |
| B | GLN130 |
| B | TYR132 |
| B | THR158 |
| B | LYS236 |
| B | SER258 |
| B | HIS260 |
| B | GLY261 |
| B | ARG263 |
| B | ASP291 |
| B | GLY292 |
| B | GLY293 |
| B | ARG295 |
| B | GLY314 |
| B | ARG315 |
| B | C7C1364 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN C 1365 |
| Chain | Residue |
| C | TYR27 |
| C | ALA79 |
| C | THR80 |
| C | ALA81 |
| C | SER108 |
| C | SER109 |
| C | GLN130 |
| C | TYR132 |
| C | THR158 |
| C | LYS236 |
| C | SER258 |
| C | HIS260 |
| C | GLY261 |
| C | ARG263 |
| C | ASP291 |
| C | GLY292 |
| C | GLY293 |
| C | ARG295 |
| C | GLY314 |
| C | ARG315 |
| C | C7C1364 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN D 1365 |
| Chain | Residue |
| D | TYR26 |
| D | TYR27 |
| D | ALA79 |
| D | THR80 |
| D | ALA81 |
| D | SER108 |
| D | SER109 |
| D | GLN130 |
| D | TYR132 |
| D | THR158 |
| D | LYS236 |
| D | SER258 |
| D | HIS260 |
| D | GLY261 |
| D | ARG263 |
| D | ASP291 |
| D | GLY292 |
| D | GLY293 |
| D | ARG295 |
| D | VAL313 |
| D | GLY314 |
| D | ARG315 |
| D | C7C1364 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE C7C A 1364 |
| Chain | Residue |
| A | TYR26 |
| A | TRP110 |
| A | TYR132 |
| A | ARG167 |
| A | TYR208 |
| A | HIS260 |
| A | ARG263 |
| A | FMN1365 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE C7C B 1364 |
| Chain | Residue |
| B | ARG167 |
| B | LEU205 |
| B | TYR208 |
| B | HIS260 |
| B | ARG263 |
| B | FMN1365 |
| B | TYR26 |
| B | MET82 |
| B | TRP110 |
| B | TYR132 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE C7C C 1364 |
| Chain | Residue |
| C | TYR26 |
| C | TRP110 |
| C | TYR132 |
| C | ARG167 |
| C | LEU205 |
| C | TYR208 |
| C | VAL209 |
| C | HIS260 |
| C | ARG263 |
| C | FMN1365 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE C7C D 1364 |
| Chain | Residue |
| D | TYR26 |
| D | TRP110 |
| D | TYR132 |
| D | ARG167 |
| D | LEU205 |
| D | TYR208 |
| D | HIS260 |
| D | ARG263 |
| D | FMN1365 |
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. SNHGARQ |
| Chain | Residue | Details |
| A | SER258-GLN264 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683 |
| Chain | Residue | Details |
| A | HIS260 | |
| B | HIS260 | |
| C | HIS260 | |
| D | HIS260 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU |
| Chain | Residue | Details |
| A | TYR26 | |
| C | TYR132 | |
| C | HIS260 | |
| C | ARG263 | |
| D | TYR26 | |
| D | TYR132 | |
| D | HIS260 | |
| D | ARG263 | |
| A | TYR132 | |
| A | HIS260 | |
| A | ARG263 | |
| B | TYR26 | |
| B | TYR132 | |
| B | HIS260 | |
| B | ARG263 | |
| C | TYR26 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U |
| Chain | Residue | Details |
| A | ALA79 | |
| B | ALA79 | |
| C | ALA79 | |
| D | ALA79 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U |
| Chain | Residue | Details |
| A | SER108 | |
| D | SER108 | |
| D | THR158 | |
| D | LYS236 | |
| A | THR158 | |
| A | LYS236 | |
| B | SER108 | |
| B | THR158 | |
| B | LYS236 | |
| C | SER108 | |
| C | THR158 | |
| C | LYS236 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00683, ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2W0U |
| Chain | Residue | Details |
| A | GLN130 | |
| B | GLN130 | |
| C | GLN130 | |
| D | GLN130 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU |
| Chain | Residue | Details |
| A | ARG167 | |
| B | ARG167 | |
| C | ARG167 | |
| D | ARG167 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|PubMed:20054120, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDT, ECO:0007744|PDB:2RDU, ECO:0007744|PDB:2RDW, ECO:0007744|PDB:2W0U |
| Chain | Residue | Details |
| A | SER258 | |
| D | SER258 | |
| D | ASP291 | |
| D | GLY314 | |
| A | ASP291 | |
| A | GLY314 | |
| B | SER258 | |
| B | ASP291 | |
| B | GLY314 | |
| C | SER258 | |
| C | ASP291 | |
| C | GLY314 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WU19 |
| Chain | Residue | Details |
| A | LYS184 | |
| B | LYS184 | |
| C | LYS184 | |
| D | LYS184 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WU19 |
| Chain | Residue | Details |
| A | SER194 | |
| B | SER194 | |
| C | SER194 | |
| D | SER194 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER230 | |
| B | SER230 | |
| C | SER230 | |
| D | SER230 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | ARG263 | |
| A | ASP160 | |
| A | HIS260 | |
| A | TYR26 | |
| A | TYR132 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | ARG263 | |
| B | ASP160 | |
| B | HIS260 | |
| B | TYR26 | |
| B | TYR132 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| C | ARG263 | |
| C | ASP160 | |
| C | HIS260 | |
| C | TYR26 | |
| C | TYR132 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| D | ARG263 | |
| D | ASP160 | |
| D | HIS260 | |
| D | TYR26 | |
| D | TYR132 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | ARG263 | |
| A | HIS260 | |
| A | ASP160 | |
| A | TYR132 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | ARG263 | |
| B | HIS260 | |
| B | ASP160 | |
| B | TYR132 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| C | ARG263 | |
| C | HIS260 | |
| C | ASP160 | |
| C | TYR132 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| D | ARG263 | |
| D | HIS260 | |
| D | ASP160 | |
| D | TYR132 |
