7R4N
Structure of human hydroxyacid oxidase 1 bound with 5-bromo-N-methyl-1H-indazole-3-carboxamide
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 |
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 | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00683 |
| Chain | Residue | Details |
| A | HIS260 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU |
| Chain | Residue | Details |
| A | TYR26 | |
| A | TYR132 | |
| A | HIS260 | |
| A | ARG263 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| 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 | |
| A | THR158 | |
| A | LYS236 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| 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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18215067, ECO:0000269|Ref.11, ECO:0007744|PDB:2NZL, ECO:0007744|PDB:2RDU |
| Chain | Residue | Details |
| A | ARG167 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| 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 | |
| A | ASP291 | |
| A | GLY314 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9WU19 |
| Chain | Residue | Details |
| A | LYS184 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WU19 |
| Chain | Residue | Details |
| A | SER194 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER230 |
