5MBX
Crystal structure of reduced murine N1-acetylpolyamine oxidase in complex with N1-acetylspermine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0006598 | biological_process | polyamine catabolic process |
| A | 0008215 | biological_process | spermine metabolic process |
| A | 0009446 | biological_process | putrescine biosynthetic process |
| A | 0009447 | biological_process | putrescine catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046203 | biological_process | spermidine catabolic process |
| A | 0046208 | biological_process | spermine catabolic process |
| A | 0046592 | molecular_function | polyamine oxidase activity |
| A | 0052899 | molecular_function | obsolete N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity |
| A | 0052901 | molecular_function | spermine oxidase activity |
| A | 0052902 | molecular_function | obsolete spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity |
| A | 0052903 | molecular_function | N(1)-acetylpolyamine oxidase (3-acetamidopropanal-forming) activity |
| A | 0052904 | molecular_function | obsolete N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity |
| A | 1901307 | biological_process | positive regulation of spermidine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 42 |
| Details | binding site for residue FAD A 1801 |
| Chain | Residue |
| A | VAL11 |
| A | GLY43 |
| A | GLY44 |
| A | ARG45 |
| A | GLY59 |
| A | ALA60 |
| A | HIS61 |
| A | TRP62 |
| A | HIS64 |
| A | PRO239 |
| A | VAL240 |
| A | GLY12 |
| A | THR279 |
| A | VAL280 |
| A | PRO281 |
| A | PHE284 |
| A | PHE292 |
| A | ASN313 |
| A | TRP420 |
| A | TYR425 |
| A | TYR430 |
| A | GLY464 |
| A | GLY14 |
| A | GLU465 |
| A | SER473 |
| A | THR474 |
| A | THR475 |
| A | ALA478 |
| A | SP51802 |
| A | HOH1913 |
| A | HOH1955 |
| A | HOH1980 |
| A | HOH1986 |
| A | ILE15 |
| A | HOH2005 |
| A | HOH2020 |
| A | HOH2062 |
| A | ALA16 |
| A | LEU36 |
| A | GLU37 |
| A | ALA38 |
| A | THR39 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue SP5 A 1802 |
| Chain | Residue |
| A | HIS64 |
| A | CYS186 |
| A | VAL187 |
| A | PHE201 |
| A | TYR204 |
| A | ASN313 |
| A | PHE375 |
| A | TYR430 |
| A | SER473 |
| A | FAD1801 |
| A | HOH1911 |
| A | HOH1940 |
| A | HOH2087 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 1803 |
| Chain | Residue |
| A | SER48 |
| A | ARG50 |
| A | GLN499 |
| A | HOH1903 |
| A | HOH2056 |
| A | HOH2100 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28029774, ECO:0007744|PDB:5LAE, ECO:0007744|PDB:5LFO, ECO:0007744|PDB:5MBX |
| Chain | Residue | Details |
| A | ALA16 | |
| A | GLU37 | |
| A | ARG45 | |
| A | HIS61 | |
| A | VAL240 | |
| A | PHE471 | |
| A | LEU480 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28029774, ECO:0007744|PDB:5MBX |
| Chain | Residue | Details |
| A | HIS64 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28029774, ECO:0007744|PDB:5LFO, ECO:0007744|PDB:5MBX |
| Chain | Residue | Details |
| A | VAL187 | |
| A | ASN313 |
