4Z25
Mimivirus R135 (residues 51-702)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 | 0016020 | cellular_component | membrane |
| 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 |
| I | 0016020 | cellular_component | membrane |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| I | 0033644 | cellular_component | host cell membrane |
| I | 0042802 | molecular_function | identical protein binding |
| I | 0044423 | cellular_component | virion component |
| I | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| J | 0016020 | cellular_component | membrane |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| J | 0033644 | cellular_component | host cell membrane |
| J | 0042802 | molecular_function | identical protein binding |
| J | 0044423 | cellular_component | virion component |
| J | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| K | 0016020 | cellular_component | membrane |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| K | 0033644 | cellular_component | host cell membrane |
| K | 0042802 | molecular_function | identical protein binding |
| K | 0044423 | cellular_component | virion component |
| K | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| L | 0016020 | cellular_component | membrane |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| L | 0033644 | cellular_component | host cell membrane |
| L | 0042802 | molecular_function | identical protein binding |
| L | 0044423 | cellular_component | virion component |
| L | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue FAD A 901 |
| Chain | Residue |
| A | GLY13 |
| A | HIS94 |
| A | GLY95 |
| A | MET96 |
| A | GLY97 |
| A | GLY100 |
| A | SER101 |
| A | ILE104 |
| A | ASN105 |
| A | ARG106 |
| A | LEU107 |
| A | GLY15 |
| A | ASN108 |
| A | ALA261 |
| A | VAL263 |
| A | THR297 |
| A | SER298 |
| A | GLY299 |
| A | SER577 |
| A | ASP605 |
| A | LEU606 |
| A | ASN616 |
| A | ALA16 |
| A | THR617 |
| A | TRP618 |
| A | ALA621 |
| A | ALA17 |
| A | GLU37 |
| A | ALA38 |
| A | SER68 |
| A | TRP75 |
| A | ALA93 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | binding site for residue FAD B 901 |
| Chain | Residue |
| B | GLY13 |
| B | GLY15 |
| B | ALA16 |
| B | ALA17 |
| B | GLU37 |
| B | ALA38 |
| 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 | ASP605 |
| B | LEU606 |
| B | ASN616 |
| B | THR617 |
| B | TRP618 |
| B | ALA621 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 901 |
| Chain | Residue |
| C | GLY13 |
| C | GLY15 |
| C | ALA16 |
| C | ALA17 |
| C | GLU37 |
| C | ALA38 |
| 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 |
| C | TRP618 |
| C | ALA621 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD D 901 |
| Chain | Residue |
| D | ALA38 |
| D | TRP75 |
| D | HIS94 |
| D | GLY95 |
| D | MET96 |
| D | GLY97 |
| D | GLY100 |
| D | SER101 |
| D | ILE104 |
| D | ASN105 |
| D | ARG106 |
| D | LEU107 |
| D | ASN108 |
| D | ALA261 |
| 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 | GLY13 |
| D | GLY15 |
| D | ALA16 |
| D | ALA17 |
| D | GLU37 |
| site_id | AC5 |
| Number of Residues | 28 |
| 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 | ASN105 |
| E | ARG106 |
| E | LEU107 |
| E | ASN108 |
| E | ALA261 |
| E | VAL263 |
| E | SER298 |
| E | SER577 |
| E | HIS578 |
| E | ASP605 |
| E | LEU606 |
| E | ASN616 |
| E | THR617 |
| E | TRP618 |
| site_id | AC6 |
| Number of Residues | 31 |
| 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 | ASN105 |
| F | ARG106 |
| F | LEU107 |
| F | ASN108 |
| F | ALA261 |
| F | VAL263 |
| F | THR297 |
| F | SER298 |
| F | GLY299 |
| F | SER577 |
| F | HIS578 |
| F | ASP605 |
| F | LEU606 |
| F | ASN616 |
| F | THR617 |
| F | TRP618 |
| F | ALA621 |
| 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 | SER68 |
| 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 | SER577 |
| G | HIS578 |
| G | ASP605 |
| G | LEU606 |
| G | ASN616 |
| G | THR617 |
| G | TRP618 |
| G | ALA621 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | binding site for residue FAD H 901 |
| Chain | Residue |
| H | GLY13 |
| H | GLY15 |
| H | ALA16 |
| H | ALA17 |
| H | GLU37 |
| H | ALA38 |
| H | TRP75 |
| 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 | VAL263 |
| H | THR297 |
| H | SER298 |
| H | GLY299 |
| H | SER577 |
| H | HIS578 |
| H | ASP605 |
| H | LEU606 |
| H | ASN616 |
| H | THR617 |
| H | TRP618 |
| H | ALA621 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | binding site for residue FAD I 901 |
| Chain | Residue |
| I | GLY13 |
| I | GLY15 |
| I | ALA16 |
| I | ALA17 |
| I | GLU37 |
| I | ALA38 |
| I | TRP75 |
| I | ALA93 |
| I | HIS94 |
| I | GLY95 |
| I | MET96 |
| I | GLY97 |
| I | GLY100 |
| I | SER101 |
| I | ILE104 |
| I | ASN105 |
| I | ARG106 |
| I | LEU107 |
| I | ASN108 |
| I | ALA261 |
| I | VAL263 |
| I | THR297 |
| I | SER298 |
| I | GLY299 |
| I | SER577 |
| I | HIS578 |
| I | ASP605 |
| I | LEU606 |
| I | ASN616 |
| I | THR617 |
| I | TRP618 |
| I | ALA621 |
| site_id | AD1 |
| Number of Residues | 30 |
| Details | binding site for residue FAD J 901 |
| Chain | Residue |
| J | GLY13 |
| J | GLY15 |
| J | ALA16 |
| J | ALA17 |
| J | GLU37 |
| J | ALA38 |
| J | TRP75 |
| J | HIS94 |
| J | GLY95 |
| J | MET96 |
| J | GLY97 |
| J | GLY100 |
| J | SER101 |
| J | ILE104 |
| J | ASN105 |
| J | ARG106 |
| J | LEU107 |
| J | ASN108 |
| J | ALA261 |
| J | VAL263 |
| J | THR297 |
| J | SER298 |
| J | SER577 |
| J | HIS578 |
| J | ASP605 |
| J | LEU606 |
| J | ASN616 |
| J | THR617 |
| J | TRP618 |
| J | ALA621 |
| site_id | AD2 |
| Number of Residues | 29 |
| Details | binding site for residue FAD K 901 |
| Chain | Residue |
| K | GLY13 |
| K | GLY15 |
| K | ALA16 |
| K | ALA17 |
| K | GLU37 |
| K | ALA38 |
| K | TRP75 |
| K | ALA93 |
| K | HIS94 |
| K | GLY95 |
| K | MET96 |
| K | GLY97 |
| K | GLY100 |
| K | SER101 |
| K | ASN105 |
| K | ARG106 |
| K | LEU107 |
| K | ASN108 |
| K | ALA261 |
| K | VAL263 |
| K | SER298 |
| K | SER577 |
| K | HIS578 |
| K | ASP605 |
| K | LEU606 |
| K | ASN616 |
| K | THR617 |
| K | TRP618 |
| K | ALA621 |
| site_id | AD3 |
| Number of Residues | 30 |
| Details | binding site for residue FAD L 901 |
| Chain | Residue |
| L | GLY13 |
| L | GLY15 |
| L | ALA16 |
| L | ALA17 |
| L | GLU37 |
| L | ALA38 |
| L | TRP75 |
| L | ALA93 |
| L | HIS94 |
| L | GLY95 |
| L | MET96 |
| L | GLY97 |
| L | GLY100 |
| L | SER101 |
| L | ILE104 |
| L | ASN105 |
| L | ARG106 |
| L | LEU107 |
| L | ASN108 |
| L | ALA261 |
| L | VAL263 |
| L | THR297 |
| L | SER298 |
| L | SER577 |
| L | HIS578 |
| L | ASP605 |
| L | LEU606 |
| L | ASN616 |
| L | THR617 |
| L | TRP618 |
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 | 240 |
| Details | TRANSMEM: Helical => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU5-LEU25 | |
| J | LEU5-LEU25 | |
| K | LEU5-LEU25 | |
| L | LEU5-LEU25 | |
| B | LEU5-LEU25 | |
| C | LEU5-LEU25 | |
| D | LEU5-LEU25 | |
| E | LEU5-LEU25 | |
| F | LEU5-LEU25 | |
| G | LEU5-LEU25 | |
| H | LEU5-LEU25 | |
| I | LEU5-LEU25 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS578 | |
| J | HIS578 | |
| K | HIS578 | |
| L | HIS578 | |
| B | HIS578 | |
| C | HIS578 | |
| D | HIS578 | |
| E | HIS578 | |
| F | HIS578 | |
| G | HIS578 | |
| H | HIS578 | |
| I | HIS578 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP8 | |
| J | ASP8 | |
| K | ASP8 | |
| L | ASP8 | |
| B | ASP8 | |
| C | ASP8 | |
| D | ASP8 | |
| E | ASP8 | |
| F | ASP8 | |
| G | ASP8 | |
| H | ASP8 | |
| I | ASP8 |
