1AL7
THREE-DIMENSIONAL STRUCTURES OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS
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 | 0009853 | biological_process | photorespiration |
| A | 0009854 | biological_process | oxidative photosynthetic carbon pathway |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 360 |
| Chain | Residue |
| A | TYR24 |
| A | LYS230 |
| A | SER252 |
| A | HIS254 |
| A | ARG257 |
| A | ASP285 |
| A | GLY286 |
| A | GLY287 |
| A | ARG289 |
| A | GLY308 |
| A | ARG309 |
| A | TYR25 |
| A | HST361 |
| A | HOH363 |
| A | HOH398 |
| A | ALA76 |
| A | PRO77 |
| A | THR78 |
| A | ALA79 |
| A | SER106 |
| A | GLN127 |
| A | THR155 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HST A 361 |
| Chain | Residue |
| A | TYR24 |
| A | TRP108 |
| A | TYR129 |
| A | TYR131 |
| A | LEU161 |
| A | ARG164 |
| A | PHE172 |
| A | ILE207 |
| A | HIS254 |
| A | ARG257 |
| A | FMN360 |
| A | HOH659 |
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 | SER252-GLN258 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2644287","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9UJM8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"2681790","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9144771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AL7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GOX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9144771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AL7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in determining the substrate specificity of glycolate oxidase","evidences":[{"source":"PubMed","id":"7705356","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"3286256","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | TYR24 | |
| A | HIS254 | |
| A | ARG257 | |
| A | TYR129 | |
| A | ASP157 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | HIS254 | |
| A | ARG257 | |
| A | TYR129 | |
| A | ASP157 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 852 |
| Chain | Residue | Details |
| A | SER106 | electrostatic stabiliser |
| A | TYR129 | electrostatic stabiliser, modifies pKa |
| A | THR155 | electrostatic stabiliser |
| A | LYS230 | electrostatic stabiliser, enhance reactivity |
| A | HIS254 | proton shuttle (general acid/base) |
