1IS2
Crystal Structure of Peroxisomal Acyl-CoA Oxidase-II from Rat Liver
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000038 | biological_process | very long-chain fatty acid metabolic process |
| A | 0003997 | molecular_function | acyl-CoA oxidase activity |
| A | 0005504 | molecular_function | fatty acid binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005778 | cellular_component | peroxisomal membrane |
| A | 0005782 | cellular_component | peroxisomal matrix |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006635 | biological_process | fatty acid beta-oxidation |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0007283 | biological_process | spermatogenesis |
| A | 0009062 | biological_process | fatty acid catabolic process |
| A | 0016401 | molecular_function | palmitoyl-CoA oxidase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0019395 | biological_process | fatty acid oxidation |
| A | 0030165 | molecular_function | PDZ domain binding |
| A | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
| A | 0055088 | biological_process | lipid homeostasis |
| A | 0071949 | molecular_function | FAD binding |
| A | 0140493 | biological_process | very long-chain fatty acid beta-oxidation |
| B | 0000038 | biological_process | very long-chain fatty acid metabolic process |
| B | 0003997 | molecular_function | acyl-CoA oxidase activity |
| B | 0005504 | molecular_function | fatty acid binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005778 | cellular_component | peroxisomal membrane |
| B | 0005782 | cellular_component | peroxisomal matrix |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006635 | biological_process | fatty acid beta-oxidation |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0007283 | biological_process | spermatogenesis |
| B | 0009062 | biological_process | fatty acid catabolic process |
| B | 0016401 | molecular_function | palmitoyl-CoA oxidase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0019395 | biological_process | fatty acid oxidation |
| B | 0030165 | molecular_function | PDZ domain binding |
| B | 0033540 | biological_process | fatty acid beta-oxidation using acyl-CoA oxidase |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
| B | 0055088 | biological_process | lipid homeostasis |
| B | 0071949 | molecular_function | FAD binding |
| B | 0140493 | biological_process | very long-chain fatty acid beta-oxidation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE FAD A 699 |
| Chain | Residue |
| A | LEU102 |
| A | PHE420 |
| A | GLU423 |
| A | THR425 |
| A | VAL426 |
| A | HOH1029 |
| A | HOH1304 |
| A | HOH1375 |
| B | ARG307 |
| B | GLN309 |
| B | SER310 |
| A | THR139 |
| B | PHE324 |
| B | THR326 |
| B | GLN327 |
| B | LYS330 |
| B | ALA395 |
| B | GLY397 |
| B | GLY398 |
| B | TYR401 |
| A | GLY144 |
| A | THR145 |
| A | TRP176 |
| A | PRO177 |
| A | GLY178 |
| A | PRO416 |
| A | THR419 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD B 1699 |
| Chain | Residue |
| A | ARG307 |
| A | SER310 |
| A | PHE324 |
| A | THR326 |
| A | GLN327 |
| A | LYS330 |
| A | ALA395 |
| A | GLY397 |
| A | GLY398 |
| A | TYR401 |
| A | HOH1033 |
| A | HOH1066 |
| B | LEU102 |
| B | THR139 |
| B | GLY144 |
| B | THR145 |
| B | TRP176 |
| B | GLY178 |
| B | ASN237 |
| B | PRO416 |
| B | THR419 |
| B | GLU423 |
| B | THR425 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pl.SNkLTYGTM |
| Chain | Residue | Details |
| A | PRO268-MET278 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11872165, ECO:0000269|PubMed:16672280 |
| Chain | Residue | Details |
| A | GLU421 | |
| B | GLU421 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11872165, ECO:0000269|PubMed:16672280 |
| Chain | Residue | Details |
| A | THR139 | |
| A | GLY178 | |
| B | THR139 | |
| B | GLY178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Cleavage => ECO:0000269|PubMed:3036800 |
| Chain | Residue | Details |
| A | VAL468 | |
| B | VAL468 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q15067 |
| Chain | Residue | Details |
| A | SER26 | |
| B | SER26 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9R0H0 |
| Chain | Residue | Details |
| A | LYS65 | |
| A | LYS216 | |
| A | LYS272 | |
| A | LYS652 | |
| B | LYS65 | |
| B | LYS216 | |
| B | LYS272 | |
| B | LYS652 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9R0H0 |
| Chain | Residue | Details |
| A | LYS89 | |
| B | ASN90 | |
| B | LYS159 | |
| B | LYS241 | |
| B | LYS349 | |
| B | LYS542 | |
| B | LYS643 | |
| B | LYS655 | |
| A | ASN90 | |
| A | LYS159 | |
| A | LYS241 | |
| A | LYS349 | |
| A | LYS542 | |
| A | LYS643 | |
| A | LYS655 | |
| B | LYS89 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q15067 |
| Chain | Residue | Details |
| A | LYS255 | |
| A | LYS267 | |
| A | LYS500 | |
| B | LYS255 | |
| B | LYS267 | |
| B | LYS500 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9R0H0 |
| Chain | Residue | Details |
| A | LYS437 | |
| A | LYS446 | |
| A | LYS512 | |
| A | LYS637 | |
| B | LYS437 | |
| B | LYS446 | |
| B | LYS512 | |
| B | LYS637 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R0H0 |
| Chain | Residue | Details |
| A | SER649 | |
| B | SER649 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | VAL281 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | VAL281 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLU421 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | GLU421 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | PHE284 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| B | PHE284 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ivh |
| Chain | Residue | Details |
| A | GLY276 |
