4Z26
Mimivirus R135 (residues 51-702)
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 | 0033644 | cellular_component | host cell membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0044423 | cellular_component | virion component |
| 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 | 0033644 | cellular_component | host cell membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0044423 | cellular_component | virion component |
| 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 | 0033644 | cellular_component | host cell membrane |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0044423 | cellular_component | virion component |
| 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 | 0033644 | cellular_component | host cell membrane |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0044423 | cellular_component | virion component |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| E | 0033644 | cellular_component | host cell membrane |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0044423 | cellular_component | virion component |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| F | 0033644 | cellular_component | host cell membrane |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0044423 | cellular_component | virion component |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| G | 0033644 | cellular_component | host cell membrane |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0044423 | cellular_component | virion component |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| H | 0033644 | cellular_component | host cell membrane |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0044423 | cellular_component | virion component |
| H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue FAD A 901 |
| Chain | Residue |
| A | GLY13 |
| A | GLY95 |
| A | MET96 |
| A | GLY97 |
| A | GLY100 |
| A | SER101 |
| A | ASN105 |
| A | ARG106 |
| A | LEU107 |
| A | ASN108 |
| A | ALA261 |
| A | GLY15 |
| A | VAL263 |
| A | THR297 |
| A | SER298 |
| A | ILE306 |
| A | SER577 |
| A | HIS578 |
| A | ASP605 |
| A | LEU606 |
| A | ASN616 |
| A | THR617 |
| A | ALA16 |
| A | TRP618 |
| A | ALA621 |
| A | HOH1001 |
| A | HOH1010 |
| A | HOH1054 |
| A | ALA17 |
| A | GLU37 |
| A | ALA38 |
| A | TRP75 |
| A | ALA93 |
| A | HIS94 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for residue FAD B 901 |
| Chain | Residue |
| B | GLY13 |
| B | GLY15 |
| B | ALA16 |
| B | ALA17 |
| B | GLU37 |
| B | ALA38 |
| B | SER68 |
| B | TRP75 |
| B | ALA93 |
| B | HIS94 |
| B | GLY95 |
| B | MET96 |
| B | GLY97 |
| B | GLY100 |
| B | SER101 |
| B | ILE104 |
| B | ASN105 |
| B | ARG106 |
| B | LEU107 |
| B | ASN108 |
| B | ALA261 |
| B | VAL263 |
| B | THR297 |
| B | SER298 |
| B | GLY299 |
| B | SER577 |
| B | HIS578 |
| B | ASP605 |
| B | LEU606 |
| B | ASN616 |
| B | THR617 |
| B | TRP618 |
| B | HOH1032 |
| B | HOH1036 |
| B | HOH1078 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | binding site for residue FAD C 901 |
| Chain | Residue |
| C | TRP618 |
| C | ALA621 |
| C | HOH1038 |
| C | GLY13 |
| C | GLY15 |
| C | ALA16 |
| C | ALA17 |
| C | GLU37 |
| C | ALA38 |
| C | SER68 |
| C | TRP75 |
| C | ALA93 |
| C | HIS94 |
| C | GLY95 |
| C | MET96 |
| C | GLY97 |
| C | GLY100 |
| C | SER101 |
| C | ASN105 |
| C | ARG106 |
| C | LEU107 |
| C | ASN108 |
| C | ALA261 |
| C | VAL263 |
| C | THR297 |
| C | SER298 |
| C | GLY299 |
| C | SER577 |
| C | HIS578 |
| C | ASP605 |
| C | LEU606 |
| C | ASN616 |
| C | THR617 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | binding site for residue FAD D 901 |
| Chain | Residue |
| D | GLY13 |
| D | GLY15 |
| D | ALA16 |
| D | ALA17 |
| D | GLU37 |
| D | ALA38 |
| D | PHE54 |
| D | TRP75 |
| D | HIS94 |
| D | GLY95 |
| D | GLY97 |
| D | GLY100 |
| D | SER101 |
| D | ASN105 |
| D | ARG106 |
| D | LEU107 |
| D | ASN108 |
| D | ALA261 |
| D | VAL262 |
| D | VAL263 |
| D | THR297 |
| D | SER298 |
| D | GLY299 |
| D | SER577 |
| D | HIS578 |
| D | ASP605 |
| D | LEU606 |
| D | ASN616 |
| D | THR617 |
| D | TRP618 |
| D | ALA621 |
| D | HOH1001 |
| D | HOH1048 |
| D | HOH1049 |
| D | HOH1090 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | binding site for residue FAD E 901 |
| Chain | Residue |
| E | GLY13 |
| E | GLY15 |
| E | ALA16 |
| E | ALA17 |
| E | GLU37 |
| E | ALA38 |
| E | TRP75 |
| E | ALA93 |
| E | HIS94 |
| E | GLY95 |
| E | MET96 |
| E | GLY97 |
| E | GLY100 |
| E | SER101 |
| E | ILE104 |
| E | ASN105 |
| E | ARG106 |
| E | LEU107 |
| E | ASN108 |
| E | ALA261 |
| E | VAL263 |
| E | THR297 |
| E | SER298 |
| E | GLY299 |
| E | SER577 |
| E | ASP605 |
| E | LEU606 |
| E | ASN616 |
| E | THR617 |
| E | TRP618 |
| E | ALA621 |
| E | HOH1015 |
| site_id | AC6 |
| Number of Residues | 32 |
| Details | binding site for residue FAD F 901 |
| Chain | Residue |
| F | GLY13 |
| F | GLY15 |
| F | ALA16 |
| F | ALA17 |
| F | GLU37 |
| F | ALA38 |
| F | TRP75 |
| F | ALA93 |
| F | HIS94 |
| F | GLY95 |
| F | MET96 |
| F | GLY97 |
| F | GLY100 |
| F | SER101 |
| F | ILE104 |
| F | ASN105 |
| F | ARG106 |
| F | ASN108 |
| F | ALA261 |
| F | VAL263 |
| F | SER298 |
| F | SER577 |
| F | HIS578 |
| F | ASP605 |
| F | LEU606 |
| F | ASN616 |
| F | THR617 |
| F | TRP618 |
| F | ALA621 |
| F | HOH1002 |
| F | HOH1005 |
| F | HOH1025 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | binding site for residue FAD G 901 |
| Chain | Residue |
| G | GLY13 |
| G | GLY15 |
| G | ALA16 |
| G | ALA17 |
| G | GLU37 |
| G | ALA38 |
| G | TRP75 |
| G | ALA93 |
| G | HIS94 |
| G | GLY95 |
| G | MET96 |
| G | GLY97 |
| G | GLY100 |
| G | SER101 |
| G | ILE104 |
| G | ASN105 |
| G | ARG106 |
| G | LEU107 |
| G | ASN108 |
| G | ALA261 |
| G | VAL263 |
| G | THR297 |
| G | SER298 |
| G | GLY299 |
| G | SER577 |
| G | HIS578 |
| G | ASP605 |
| G | LEU606 |
| G | ASN616 |
| G | THR617 |
| G | TRP618 |
| G | ALA621 |
| site_id | AC8 |
| Number of Residues | 39 |
| Details | binding site for residue FAD H 901 |
| Chain | Residue |
| H | ILE12 |
| H | GLY13 |
| H | GLY15 |
| H | ALA16 |
| H | ALA17 |
| H | LEU36 |
| H | GLU37 |
| H | ALA38 |
| H | SER68 |
| H | TRP75 |
| H | ALA93 |
| H | HIS94 |
| H | GLY95 |
| H | MET96 |
| H | GLY97 |
| H | GLY100 |
| H | SER101 |
| H | ILE104 |
| H | ASN105 |
| H | ARG106 |
| H | LEU107 |
| H | ASN108 |
| H | ALA261 |
| H | VAL262 |
| H | VAL263 |
| H | THR297 |
| H | SER298 |
| H | GLY299 |
| H | SER577 |
| H | HIS578 |
| H | ASP605 |
| H | LEU606 |
| H | ASN616 |
| H | THR617 |
| H | TRP618 |
| H | HOH1001 |
| H | HOH1002 |
| H | HOH1006 |
| H | HOH1045 |
Functional Information from PROSITE/UniProt
| site_id | PS00624 |
| Number of Residues | 15 |
| Details | GMC_OXRED_2 GMC oxidoreductases signature 2. GAfyTPtILqrSGIG |
| Chain | Residue | Details |
| A | GLY299-GLY313 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 240 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






