6GMB
Structure of human hydroxyacid oxidase 1 bound with FMN and glycolate
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 | 6 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | LEU37 |
A | ILE41 |
A | HOH618 |
A | HOH627 |
A | HOH633 |
A | HOH723 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | GLU287 |
A | PHE323 |
A | GLN324 |
A | LYS327 |
A | HOH764 |
A | HOH890 |
A | GLY284 |
A | LYS285 |
A | VAL286 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue PG4 A 503 |
Chain | Residue |
A | GLU12 |
A | ARG295 |
A | ARG315 |
A | TRP319 |
A | HOH612 |
A | HOH622 |
A | HOH736 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | CYS7 |
A | ASN32 |
A | ASP33 |
A | LYS296 |
A | GLU339 |
A | HOH860 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LEU54 |
A | ARG55 |
A | SER218 |
A | TRP219 |
A | HOH636 |
site_id | AC6 |
Number of Residues | 24 |
Details | binding site for residue FMN A 506 |
Chain | Residue |
A | TYR26 |
A | TYR27 |
A | ALA79 |
A | THR80 |
A | ALA81 |
A | SER108 |
A | GLN130 |
A | TYR132 |
A | THR158 |
A | LYS236 |
A | SER258 |
A | HIS260 |
A | GLY261 |
A | ARG263 |
A | ASP291 |
A | GLY292 |
A | GLY293 |
A | ARG295 |
A | GLY314 |
A | ARG315 |
A | GOA507 |
A | HOH628 |
A | HOH746 |
A | HOH753 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue GOA A 507 |
Chain | Residue |
A | TYR26 |
A | TRP110 |
A | TYR132 |
A | ARG167 |
A | LEU205 |
A | HIS260 |
A | ARG263 |
A | FMN506 |
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 |