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3DAX

Crystal structure of human CYP7A1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006699biological_processbile acid biosynthetic process
A0006707biological_processcholesterol catabolic process
A0008123molecular_functioncholesterol 7-alpha-monooxygenase activity
A0008203biological_processcholesterol metabolic process
A0014070biological_processresponse to organic cyclic compound
A0015721biological_processbile acid and bile salt transport
A0016020cellular_componentmembrane
A0016125biological_processsterol metabolic process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0032966biological_processnegative regulation of collagen biosynthetic process
A0033782molecular_function24-hydroxycholesterol 7alpha-hydroxylase activity
A0038183biological_processbile acid signaling pathway
A0042632biological_processcholesterol homeostasis
A0043231cellular_componentintracellular membrane-bounded organelle
A0045471biological_processresponse to ethanol
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045717biological_processnegative regulation of fatty acid biosynthetic process
A0046872molecular_functionmetal ion binding
A0070857biological_processregulation of bile acid biosynthetic process
A0071333biological_processcellular response to glucose stimulus
A0071397biological_processcellular response to cholesterol
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006699biological_processbile acid biosynthetic process
B0006707biological_processcholesterol catabolic process
B0008123molecular_functioncholesterol 7-alpha-monooxygenase activity
B0008203biological_processcholesterol metabolic process
B0014070biological_processresponse to organic cyclic compound
B0015721biological_processbile acid and bile salt transport
B0016020cellular_componentmembrane
B0016125biological_processsterol metabolic process
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0032966biological_processnegative regulation of collagen biosynthetic process
B0033782molecular_function24-hydroxycholesterol 7alpha-hydroxylase activity
B0038183biological_processbile acid signaling pathway
B0042632biological_processcholesterol homeostasis
B0043231cellular_componentintracellular membrane-bounded organelle
B0045471biological_processresponse to ethanol
B0045542biological_processpositive regulation of cholesterol biosynthetic process
B0045717biological_processnegative regulation of fatty acid biosynthetic process
B0046872molecular_functionmetal ion binding
B0070857biological_processregulation of bile acid biosynthetic process
B0071333biological_processcellular response to glucose stimulus
B0071397biological_processcellular response to cholesterol
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 601
ChainResidue
AHIS101
APHE437
ATHR442
ACYS444
APRO445
AALA450
AGLU453
AHOH659
APHE129
AALA285
ASER286
AASN289
ATHR290
AALA293
ASER360
APRO436

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE HEM B 601
ChainResidue
BHIS101
BPHE129
BALA285
BASN289
BTHR290
BALA293
BSER360
BPRO436
BPHE437
BTHR442
BCYS444
BPRO445
BALA450
BGLU453

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX A 1
ChainResidue
AALA285
AASN289

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX B 2
ChainResidue
BALA285
BASN289

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGATICPG
ChainResidueDetails
APHE437-GLY446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0007744|PDB:3DAX
ChainResidueDetails
ACYS444
BCYS444

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PDB entries from 2024-07-24

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