1E1L
STRUCTURE OF ADRENODOXIN REDUCTASE IN COMPLEX WITH NADP obtained by cocrystallisation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0015039 | molecular_function | NADPH-adrenodoxin reductase activity |
| 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 |
| A | 0070995 | biological_process | NADPH oxidation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD A 801 |
| Chain | Residue |
| A | GLY13 |
| A | VAL82 |
| A | SER101 |
| A | TYR102 |
| A | GLY103 |
| A | TYR331 |
| A | TRP367 |
| A | GLY374 |
| A | VAL375 |
| A | ILE376 |
| A | THR379 |
| A | GLY15 |
| A | NAP802 |
| A | HOH2002 |
| A | HOH2079 |
| A | HOH2101 |
| A | HOH2103 |
| A | HOH2104 |
| A | HOH2105 |
| A | PRO16 |
| A | ALA17 |
| A | GLU38 |
| A | LYS39 |
| A | GLY45 |
| A | LEU46 |
| A | GLY50 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP A 802 |
| Chain | Residue |
| A | GLY152 |
| A | GLN153 |
| A | GLY154 |
| A | ASN155 |
| A | VAL156 |
| A | ARG197 |
| A | ARG198 |
| A | GLU209 |
| A | ILE329 |
| A | TRP367 |
| A | THR373 |
| A | GLY374 |
| A | VAL375 |
| A | FAD801 |
| A | HOH2068 |
| A | HOH2106 |
| A | HOH2107 |
| A | HOH2108 |
| A | HOH2109 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10369776 |
| Chain | Residue | Details |
| A | ALA17 | |
| A | GLU38 | |
| A | LEU46 | |
| A | VAL82 | |
| A | TRP367 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10998235 |
| Chain | Residue | Details |
| A | GLN153 | |
| A | ARG197 | |
| A | GLU209 | |
| A | GLY374 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P22570 |
| Chain | Residue | Details |
| A | SER279 | |
| A | SER286 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1e6e |
| Chain | Residue | Details |
| A | THR377 | |
| A | ILE376 | |
| A | HIS55 | |
| A | 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 |
