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 | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006696 | biological_process | ergosterol biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic 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 | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006694 | biological_process | steroid biosynthetic process |
| B | 0006696 | biological_process | ergosterol biosynthetic process |
| B | 0008202 | biological_process | steroid metabolic 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 | 286 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 526 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16407065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19483672","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16407065","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16407065","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
