4MIF
Pyranose 2-oxidase from Phanerochaete chrysosporium, wild type from natural source
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0050233 | molecular_function | pyranose oxidase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0050233 | molecular_function | pyranose oxidase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0050233 | molecular_function | pyranose oxidase activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0050233 | molecular_function | pyranose oxidase activity |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FDA A 801 |
| Chain | Residue |
| A | GLY20 |
| A | GLY151 |
| A | GLY154 |
| A | MET155 |
| A | HIS158 |
| A | TRP159 |
| A | THR160 |
| A | CYS161 |
| A | ALA162 |
| A | HIS281 |
| A | CYS283 |
| A | GLY22 |
| A | CYS332 |
| A | ALA336 |
| A | VAL340 |
| A | LEU552 |
| A | GLY585 |
| A | ASN586 |
| A | ASN596 |
| A | PRO597 |
| A | THR598 |
| A | HOH915 |
| A | PRO23 |
| A | HOH925 |
| A | HOH930 |
| A | HOH947 |
| A | HOH973 |
| A | HOH1099 |
| A | HOH1100 |
| A | HOH1258 |
| A | ILE24 |
| A | GLU43 |
| A | ILE44 |
| A | ILE96 |
| A | THR149 |
| A | ARG150 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FDA B 801 |
| Chain | Residue |
| B | GLY20 |
| B | GLY22 |
| B | PRO23 |
| B | ILE24 |
| B | GLU43 |
| B | ILE44 |
| B | THR149 |
| B | ARG150 |
| B | GLY151 |
| B | GLY154 |
| B | MET155 |
| B | HIS158 |
| B | TRP159 |
| B | THR160 |
| B | CYS161 |
| B | ALA162 |
| B | CYS283 |
| B | CYS332 |
| B | ALA336 |
| B | VAL340 |
| B | LEU552 |
| B | HIS553 |
| B | GLY585 |
| B | ASN586 |
| B | ASN596 |
| B | PRO597 |
| B | THR598 |
| B | HOH937 |
| B | HOH945 |
| B | HOH951 |
| B | HOH968 |
| B | HOH969 |
| B | HOH993 |
| B | HOH1020 |
| B | HOH1120 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 802 |
| Chain | Residue |
| B | GLU202 |
| B | HOH901 |
| B | HOH902 |
| B | HOH903 |
| B | HOH904 |
| D | ASN577 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FDA C 801 |
| Chain | Residue |
| C | LEU552 |
| C | GLY585 |
| C | ASN586 |
| C | ASN596 |
| C | PRO597 |
| C | THR598 |
| C | HOH912 |
| C | HOH920 |
| C | HOH922 |
| C | HOH937 |
| C | HOH942 |
| C | HOH952 |
| C | HOH1085 |
| C | GLY20 |
| C | GLY22 |
| C | PRO23 |
| C | ILE24 |
| C | GLU43 |
| C | ILE44 |
| C | THR149 |
| C | ARG150 |
| C | GLY151 |
| C | GLY154 |
| C | MET155 |
| C | SER156 |
| C | HIS158 |
| C | TRP159 |
| C | THR160 |
| C | CYS161 |
| C | ALA162 |
| C | CYS283 |
| C | CYS332 |
| C | GLY333 |
| C | ALA336 |
| C | VAL340 |
| site_id | AC5 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FDA D 801 |
| Chain | Residue |
| D | GLY20 |
| D | GLY22 |
| D | PRO23 |
| D | ILE24 |
| D | GLU43 |
| D | ILE44 |
| D | ILE96 |
| D | THR149 |
| D | ARG150 |
| D | GLY151 |
| D | GLY154 |
| D | MET155 |
| D | HIS158 |
| D | TRP159 |
| D | THR160 |
| D | CYS161 |
| D | ALA162 |
| D | HIS281 |
| D | CYS283 |
| D | CYS332 |
| D | ALA336 |
| D | VAL340 |
| D | LEU552 |
| D | GLY585 |
| D | ASN586 |
| D | ASN596 |
| D | PRO597 |
| D | THR598 |
| D | HOH930 |
| D | HOH932 |
| D | HOH933 |
| D | HOH938 |
| D | HOH984 |
| D | HOH1000 |
| D | HOH1010 |
| D | HOH1273 |
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. VVRNPPW |
| Chain | Residue | Details |
| A | VAL402-TRP408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:E4QP00 |
| Chain | Residue | Details |
| A | HIS553 | |
| B | HIS553 | |
| C | HIS553 | |
| D | HIS553 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ASN596 | |
| B | ASN596 | |
| C | ASN596 | |
| D | ASN596 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLN454 | |
| A | HIS456 | |
| B | GLN454 | |
| B | HIS456 | |
| C | GLN454 | |
| C | HIS456 | |
| D | GLN454 | |
| D | HIS456 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Tele-8alpha-FAD histidine => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS158 | |
| B | HIS158 | |
| C | HIS158 | |
| D | HIS158 |
