7R4O
Structure of human hydroxyacid oxidase 1 bound with 2-((4H-1,2,4-triazol-3-yl)thio)-1-(4-(3-chlorophenyl)piperazin-1-yl)ethan-1-one
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 | 0019395 | biological_process | fatty acid oxidation |
| 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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human hydroxyacid oxidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00683","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human hydroxyacid oxidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18215067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20054120","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human hydroxyacid oxidase 1.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2NZL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W0U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WU19","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
