Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7MK8

Crystal structure of a surface mutant of human fetal-specific CYP3A7 bound to dithiothreitol

Functional Information from GO Data
ChainGOidnamespacecontents
A0002933biological_processlipid hydroxylation
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006694biological_processsteroid biosynthetic process
A0006805biological_processxenobiotic metabolic process
A0008202biological_processsteroid metabolic process
A0008210biological_processestrogen metabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0008401molecular_functionretinoic acid 4-hydroxylase activity
A0016020cellular_componentmembrane
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0042572biological_processretinol metabolic process
A0042573biological_processretinoic acid metabolic process
A0046872molecular_functionmetal ion binding
A0050649molecular_functiontestosterone 6-beta-hydroxylase activity
A0062183molecular_functionall-trans retinoic acid 18-hydroxylase activity
A0070330molecular_functionaromatase activity
A0070989biological_processoxidative demethylation
A0101020molecular_functionestrogen 16-alpha-hydroxylase activity
A0101021molecular_functionestrogen 2-hydroxylase activity
B0002933biological_processlipid hydroxylation
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006694biological_processsteroid biosynthetic process
B0006805biological_processxenobiotic metabolic process
B0008202biological_processsteroid metabolic process
B0008210biological_processestrogen metabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0008401molecular_functionretinoic acid 4-hydroxylase activity
B0016020cellular_componentmembrane
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0042572biological_processretinol metabolic process
B0042573biological_processretinoic acid metabolic process
B0046872molecular_functionmetal ion binding
B0050649molecular_functiontestosterone 6-beta-hydroxylase activity
B0062183molecular_functionall-trans retinoic acid 18-hydroxylase activity
B0070330molecular_functionaromatase activity
B0070989biological_processoxidative demethylation
B0101020molecular_functionestrogen 16-alpha-hydroxylase activity
B0101021molecular_functionestrogen 2-hydroxylase activity
Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGPRNCIG
ChainResidueDetails
APHE435-GLY444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250
ChainResidueDetails
ACYS442
BCYS442

223532

PDB entries from 2024-08-07

PDB statisticsPDBj update infoContact PDBjnumon