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2Q9F

Crystal structure of human cytochrome P450 46A1 in complex with cholesterol-3-sulphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006699biological_processbile acid biosynthetic process
A0006707biological_processcholesterol catabolic process
A0006805biological_processxenobiotic metabolic process
A0007399biological_processnervous system development
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008207biological_processC21-steroid hormone metabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016020cellular_componentmembrane
A0016125biological_processsterol metabolic process
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0030425cellular_componentdendrite
A0033781molecular_functioncholesterol 24-hydroxylase activity
A0042448biological_processprogesterone metabolic process
A0042995cellular_componentcell projection
A0045202cellular_componentsynapse
A0046872molecular_functionmetal ion binding
A0050649molecular_functiontestosterone 6-beta-hydroxylase activity
A0062184molecular_functiontestosterone 16-beta-hydroxylase activity
A0065008biological_processregulation of biological quality
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A1900271biological_processregulation of long-term synaptic potentiation
A1903044biological_processprotein localization to membrane raft
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 601
ChainResidue
AGLY198
AMET199
AARG261
AHOH786

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 602
ChainResidue
APHE299
AALA302
AGLY303
ATHR306
ASER307
AALA367
ATHR370
APRO429
APHE430
ASER431
AARG435
ACYS437
AILE438
APHE442
AALA443
AHOH712
AHOH715
AHOH732
ALYS104
ATYR109
ALEU125
ATRP134
AARG138

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE C3S A 600
ChainResidue
APHE80
AHIS81
AMET108
ATYR109
AARG110
AARG226
AASN227
AALA474

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 931
ChainResidue
ASER92
ALYS94
ALYS95
AASP381
AHOH763

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 932
ChainResidue
ATRP67
AGLU334
AARG349
AGLN351

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 933
ChainResidue
AASN78
APHE80
ALYS82
ATHR83
ASER338
ALYS339

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 934
ChainResidue
APRO423
APHE425
AHOH737

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 935
ChainResidue
AMET183
ALEU204
ALYS209

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 936
ChainResidue
ALYS171
ASER179
AASP182

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSlGHRSCIG
ChainResidueDetails
APHE430-GLY439

Functional Information from SwissProt/UniProt
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
ATHR306
AGLU305

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PDB entries from 2025-06-11

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