1E6E
ADRENODOXIN REDUCTASE/ADRENODOXIN COMPLEX OF MITOCHONDRIAL P450 SYSTEMS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006744 | biological_process | ubiquinone biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0022900 | biological_process | electron transport chain |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0140647 | biological_process | P450-containing electron transport chain |
| C | 0004324 | molecular_function | ferredoxin-NADP+ reductase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005743 | cellular_component | mitochondrial inner membrane |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006694 | biological_process | steroid biosynthetic process |
| C | 0006744 | biological_process | ubiquinone biosynthetic process |
| C | 0008202 | biological_process | steroid metabolic process |
| C | 0008203 | biological_process | cholesterol metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0022900 | biological_process | electron transport chain |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050661 | molecular_function | NADP binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0140647 | biological_process | P450-containing electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3001 |
| Chain | Residue |
| A | CYS74 |
| A | PHE76 |
| A | SER423 |
| A | PHE424 |
| A | SER425 |
| A | HOH2016 |
| A | HOH2020 |
| A | HOH2127 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3004 |
| Chain | Residue |
| A | ARG73 |
| A | SER71 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3005 |
| Chain | Residue |
| A | ARG334 |
| C | ARG278 |
| C | HOH2083 |
| C | HOH2089 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3002 |
| Chain | Residue |
| C | CYS74 |
| C | PHE76 |
| C | SER423 |
| C | PHE424 |
| C | SER425 |
| C | HOH2014 |
| C | HOH2111 |
| C | HOH2123 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3003 |
| Chain | Residue |
| C | SER71 |
| C | ASP72 |
| C | ARG73 |
| site_id | AC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD A 461 |
| Chain | Residue |
| A | GLY13 |
| A | GLY15 |
| A | PRO16 |
| A | ALA17 |
| A | GLU38 |
| A | LYS39 |
| A | GLY45 |
| A | LEU46 |
| A | GLY50 |
| A | VAL58 |
| A | VAL80 |
| A | VAL82 |
| A | SER101 |
| A | TYR102 |
| A | GLY103 |
| A | GLU105 |
| A | ARG124 |
| A | VAL127 |
| A | ASP159 |
| A | ILE336 |
| A | GLY366 |
| A | TRP367 |
| A | GLY374 |
| A | VAL375 |
| A | ILE376 |
| A | THR379 |
| A | HOH2046 |
| A | HOH2047 |
| A | HOH2124 |
| A | HOH2125 |
| A | HOH2126 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES B 129 |
| Chain | Residue |
| B | GLY44 |
| B | CYS46 |
| B | GLY48 |
| B | LEU50 |
| B | CYS52 |
| B | CYS55 |
| B | CYS92 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD C 461 |
| Chain | Residue |
| C | GLY13 |
| C | GLY15 |
| C | PRO16 |
| C | ALA17 |
| C | GLU38 |
| C | LYS39 |
| C | GLN40 |
| C | GLY45 |
| C | LEU46 |
| C | GLY50 |
| C | HIS55 |
| C | VAL58 |
| C | VAL80 |
| C | VAL82 |
| C | SER101 |
| C | TYR102 |
| C | GLY103 |
| C | GLU105 |
| C | ASP159 |
| C | ILE336 |
| C | GLY366 |
| C | TRP367 |
| C | GLY374 |
| C | VAL375 |
| C | ILE376 |
| C | THR379 |
| C | HOH2009 |
| C | HOH2019 |
| C | HOH2021 |
| C | HOH2041 |
| C | HOH2118 |
| C | HOH2119 |
| C | HOH2120 |
| C | HOH2122 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES D 129 |
| Chain | Residue |
| D | GLY48 |
| D | LEU50 |
| D | CYS52 |
| D | CYS55 |
| D | CYS92 |
| D | GLY44 |
| D | CYS46 |
Functional Information from PROSITE/UniProt
| site_id | PS00814 |
| Number of Residues | 11 |
| Details | ADX Adrenodoxin family, iron-sulfur binding region signature. CegTlACSTCH |
| Chain | Residue | Details |
| B | CYS46-HIS56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10369776","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10998235","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P22570","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 104 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P46656","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P46656","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P10109","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 11053423, 12069587, 10998235 |
| Chain | Residue | Details |
| A | THR377 | |
| A | THR377 | |
| A | ILE376 | |
| A | ILE376 | |
| A | HIS55 | |
| A | ASP159 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 11053423, 12069587, 10998235 |
| Chain | Residue | Details |
| C | THR377 | |
| C | THR377 | |
| C | ILE376 | |
| C | ILE376 | |
| C | HIS55 | |
| C | ASP159 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 142 |
| Chain | Residue | Details |
| A | HIS55 | electrostatic stabiliser, hydrogen bond acceptor |
| A | ASP159 | electrostatic stabiliser, hydrogen bond acceptor |
| A | ILE376 | polar interaction, single electron acceptor, single electron donor, single electron relay |
| A | THR377 | polar interaction, single electron acceptor, single electron donor, single electron relay |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 142 |
| Chain | Residue | Details |
| C | HIS55 | electrostatic stabiliser, hydrogen bond acceptor |
| C | ASP159 | electrostatic stabiliser, hydrogen bond acceptor |
| C | ILE376 | polar interaction, single electron acceptor, single electron donor, single electron relay |
| C | THR377 | polar interaction, single electron acceptor, single electron donor, single electron relay |






