1CJC
STRUCTURE OF ADRENODOXIN REDUCTASE 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 | 0016020 | cellular_component | membrane |
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 | 30 |
Details | BINDING SITE FOR RESIDUE FAD A 1058 |
Chain | Residue |
A | GLY13 |
A | VAL58 |
A | VAL82 |
A | SER101 |
A | TYR102 |
A | GLY103 |
A | GLU105 |
A | TRP367 |
A | GLY374 |
A | VAL375 |
A | ILE376 |
A | GLY15 |
A | THR379 |
A | HOH1059 |
A | HOH1064 |
A | HOH1067 |
A | HOH1071 |
A | HOH1074 |
A | HOH1083 |
A | HOH1113 |
A | HOH1130 |
A | HOH1320 |
A | PRO16 |
A | HOH1493 |
A | ALA17 |
A | GLU38 |
A | LYS39 |
A | GLY45 |
A | LEU46 |
A | GLY50 |
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 |