1E1K
ADRENODOXIN REDUCTASE in complex with NADP+ obtained by a soaking experiment
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 801 |
| Chain | Residue |
| A | GLY13 |
| A | GLY50 |
| A | VAL58 |
| A | VAL82 |
| A | SER101 |
| A | TYR102 |
| A | GLY103 |
| A | GLU105 |
| A | GLY366 |
| A | TRP367 |
| A | GLY374 |
| A | GLY15 |
| A | VAL375 |
| A | ILE376 |
| A | THR379 |
| A | NAP802 |
| A | HOH2036 |
| A | HOH2091 |
| A | HOH2136 |
| A | HOH2285 |
| A | HOH2331 |
| A | HOH2332 |
| A | PRO16 |
| A | HOH2333 |
| A | HOH2334 |
| A | HOH2335 |
| A | HOH2337 |
| A | ALA17 |
| A | GLU38 |
| A | LYS39 |
| A | GLN40 |
| A | GLY45 |
| A | LEU46 |
| site_id | AC2 |
| Number of Residues | 30 |
| 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 | PRO280 |
| A | SER328 |
| A | ILE329 |
| A | TYR331 |
| A | TRP367 |
| A | PRO372 |
| A | THR373 |
| A | VAL375 |
| A | FAD801 |
| A | HOH2100 |
| A | HOH2167 |
| A | HOH2172 |
| A | HOH2175 |
| A | HOH2267 |
| A | HOH2338 |
| A | HOH2339 |
| A | HOH2341 |
| A | HOH2342 |
| A | HOH2343 |
| A | HOH2344 |
| A | HOH2345 |
| A | HOH2346 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10369776","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10998235","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P22570","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
