7M2O
Crystal structure of Human Glycolate Oxidase with Inhibitor Compound 15
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 PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue FMN A 401 |
| Chain | Residue |
| A | TYR27 |
| A | LYS236 |
| A | SER258 |
| A | HIS260 |
| A | GLY261 |
| A | ARG263 |
| A | ASP291 |
| A | GLY292 |
| A | GLY293 |
| A | ARG295 |
| A | GLY314 |
| A | ALA79 |
| A | ARG315 |
| A | YOJ402 |
| A | HOH550 |
| A | HOH574 |
| A | HOH634 |
| A | THR80 |
| A | ALA81 |
| A | SER108 |
| A | TRP110 |
| A | GLN130 |
| A | TYR132 |
| A | THR158 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue YOJ A 402 |
| Chain | Residue |
| A | TYR26 |
| A | ALA81 |
| A | MET82 |
| A | TRP110 |
| A | ALA111 |
| A | THR112 |
| A | SER113 |
| A | SER114 |
| A | TYR132 |
| A | TYR134 |
| A | ARG167 |
| A | LEU205 |
| A | TYR208 |
| A | HIS260 |
| A | ARG263 |
| A | FMN401 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ASN32 |
| A | ASP33 |
| A | LEU168 |
| A | GLU339 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PEG A 404 |
| Chain | Residue |
| A | ASP61 |
| A | SER63 |
| A | ASN351 |
| A | LYS353 |
| A | HOH511 |
| A | HOH543 |
| A | HOH645 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ALA281 |
| A | GLU283 |
| A | LYS285 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ARG52 |
| A | MET53 |
| A | LEU54 |
| A | ARG55 |
| A | VAL159 |
| A | ALA345 |
| A | GLY348 |
| A | HOH648 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue PEG A 407 |
| Chain | Residue |
| A | ARG84 |
| A | MET85 |
| A | ALA86 |
| A | HIS87 |
| A | VAL88 |
| A | LYS353 |
| A | HOH502 |
| A | HOH579 |
| A | HOH645 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 408 |
| Chain | Residue |
| A | LEU5 |
| A | GLN13 |
| A | HOH557 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | LEU37 |
| A | ALA38 |
| A | ILE41 |
| A | HOH539 |
| A | HOH600 |
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 | HIS260 | |
| A | ARG263 | |
| A | TYR26 | |
| A | TYR132 |
| 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 | ASP291 | |
| A | GLY314 | |
| A | SER258 |
| 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 |
