4Z26
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 |
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 | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | LEU5-LEU25 | |
B | LEU5-LEU25 | |
C | LEU5-LEU25 | |
D | LEU5-LEU25 | |
E | LEU5-LEU25 | |
F | LEU5-LEU25 | |
G | LEU5-LEU25 | |
H | LEU5-LEU25 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | ACT_SITE: ACT_SITE => ECO:0000250 |
Chain | Residue | Details |
A | HIS578 | |
B | HIS578 | |
C | HIS578 | |
D | HIS578 | |
E | HIS578 | |
F | HIS578 | |
G | HIS578 | |
H | HIS578 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP8 | |
B | ASP8 | |
C | ASP8 | |
D | ASP8 | |
E | ASP8 | |
F | ASP8 | |
G | ASP8 | |
H | ASP8 |