2BF4
A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
A | 0003959 | molecular_function | NADPH dehydrogenase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005741 | cellular_component | mitochondrial outer membrane |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006696 | biological_process | ergosterol biosynthetic process |
A | 0009055 | molecular_function | electron transfer activity |
A | 0010181 | molecular_function | FMN binding |
A | 0016126 | biological_process | sterol biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050661 | molecular_function | NADP binding |
B | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
B | 0003959 | molecular_function | NADPH dehydrogenase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005741 | cellular_component | mitochondrial outer membrane |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006696 | biological_process | ergosterol biosynthetic process |
B | 0009055 | molecular_function | electron transfer activity |
B | 0010181 | molecular_function | FMN binding |
B | 0016126 | biological_process | sterol biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 760 |
Chain | Residue |
A | SER282 |
A | ASP284 |
A | ARG285 |
A | ASN582 |
A | HOH2107 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 761 |
Chain | Residue |
A | ASP626 |
B | PRO337 |
B | LEU338 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 762 |
Chain | Residue |
B | ARG553 |
site_id | AC4 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE FAD A 750 |
Chain | Residue |
A | HIS306 |
A | GLY364 |
A | PRO365 |
A | TYR405 |
A | PHE406 |
A | ASN407 |
A | ARG439 |
A | TYR440 |
A | TYR441 |
A | SER442 |
A | THR457 |
A | SER458 |
A | ILE459 |
A | GLU461 |
A | PHE463 |
A | VAL474 |
A | VAL475 |
A | GLY476 |
A | VAL477 |
A | THR478 |
A | THR479 |
A | TRP691 |
A | FMN751 |
A | FMN752 |
A | HOH2060 |
A | HOH2096 |
A | HOH2097 |
A | HOH2098 |
A | HOH2101 |
A | HOH2106 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FMN A 751 |
Chain | Residue |
A | SER67 |
A | GLN68 |
A | THR69 |
A | GLY70 |
A | THR71 |
A | ALA72 |
A | SER116 |
A | THR117 |
A | TYR118 |
A | GLY119 |
A | GLU120 |
A | LEU152 |
A | GLY153 |
A | ASN154 |
A | TYR157 |
A | GLU158 |
A | PHE159 |
A | PHE160 |
A | ASN161 |
A | VAL690 |
A | FAD750 |
A | HOH2103 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE FMN A 752 |
Chain | Residue |
A | THR69 |
A | ASP74 |
A | TYR75 |
A | LYS78 |
A | ASP187 |
A | ASP193 |
A | PRO365 |
A | VAL366 |
A | SER367 |
A | FAD750 |
A | HOH2033 |
A | HOH2096 |
A | HOH2100 |
A | HOH2101 |
A | HOH2103 |
A | HOH2104 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAP A 753 |
Chain | Residue |
A | ARG285 |
A | ILE459 |
A | GLU461 |
A | PRO541 |
A | GLY542 |
A | THR543 |
A | SER580 |
A | ARG581 |
A | SER610 |
A | ARG611 |
A | LYS617 |
A | TYR619 |
A | GLN621 |
A | ASP646 |
A | GLY649 |
A | MET650 |
A | HOH2080 |
A | HOH2105 |
A | HOH2106 |
site_id | AC8 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FAD B 750 |
Chain | Residue |
B | TYR405 |
B | PHE406 |
B | ASN407 |
B | ARG439 |
B | TYR440 |
B | TYR441 |
B | SER442 |
B | THR457 |
B | SER458 |
B | ILE459 |
B | GLU461 |
B | VAL474 |
B | VAL475 |
B | GLY476 |
B | VAL477 |
B | THR478 |
B | THR479 |
B | TRP691 |
B | FMN751 |
B | FMN752 |
B | HOH2043 |
B | HIS306 |
B | GLY364 |
B | PRO365 |
site_id | AC9 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE FMN B 751 |
Chain | Residue |
B | SER67 |
B | GLN68 |
B | THR69 |
B | GLY70 |
B | THR71 |
B | ALA72 |
B | SER116 |
B | THR117 |
B | TYR118 |
B | GLY119 |
B | LEU152 |
B | GLY153 |
B | ASN154 |
B | TYR157 |
B | PHE159 |
B | PHE160 |
B | ASN161 |
B | ASP187 |
B | VAL690 |
B | FAD750 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FMN B 752 |
Chain | Residue |
B | THR71 |
B | ASP74 |
B | TYR75 |
B | LYS78 |
B | ASP187 |
B | ASP193 |
B | PRO365 |
B | VAL366 |
B | SER367 |
B | PRO434 |
B | FAD750 |
B | HOH2008 |
B | HOH2043 |
site_id | BC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NAP B 753 |
Chain | Residue |
B | ARG285 |
B | ILE459 |
B | GLU461 |
B | PRO541 |
B | GLY542 |
B | THR543 |
B | SER580 |
B | ARG581 |
B | SER610 |
B | ARG611 |
B | LYS617 |
B | TYR619 |
B | GLN621 |
B | ASP646 |
B | GLY649 |
B | MET650 |
B | TRP691 |
B | HOH2020 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1332 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
A | PRO25-TRP691 | |
B | PRO25-TRP691 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672 |
Chain | Residue | Details |
A | GLN68 | |
A | THR117 | |
A | GLY153 | |
B | GLN68 | |
B | THR117 | |
B | GLY153 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16407065 |
Chain | Residue | Details |
A | PHE79 | |
A | ALA647 | |
B | PHE79 | |
B | ALA647 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16407065 |
Chain | Residue | Details |
A | GLY188 | |
B | GLY188 | |
B | ASN286 | |
B | TYR440 | |
B | SER458 | |
B | VAL477 | |
B | GLY544 | |
B | ARG611 | |
B | VAL618 | |
B | TRP691 | |
A | ASN286 | |
A | TYR440 | |
A | SER458 | |
A | VAL477 | |
A | GLY544 | |
A | ARG611 | |
A | VAL618 | |
A | TRP691 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 |
Chain | Residue | Details |
A | SER667 | |
B | SER667 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ndh |
Chain | Residue | Details |
A | SER444 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ndh |
Chain | Residue | Details |
B | SER444 |