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3V8D

Crystal structure of human CYP7A1 in complex with 7-ketocholesterol

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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 601
ChainResidue
AHIS101
AASN362
APRO436
APHE437
ATHR442
AILE443
ACYS444
APRO445
AALA450
AGLU453
AILE488
APHE129
A0GV602
AHOH701
AHOH798
AHOH805
AHOH843
ALEU133
AALA285
ASER286
AASN289
ATHR290
AALA293
ASER360

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0GV A 602
ChainResidue
AHIS101
AILE114
AILE125
AARG260
ATRP284
AALA285
ASER360
ALEU361
AGLY485
ALEU486
AHEM601
AHOH701

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 603
ChainResidue
AHIS65
AVAL66
AASN81
ASER84
ALEU374
AASP376
AGLY377
ATYR379
AHOH707
AHOH750

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 604
ChainResidue
ALYS500
APHE501
ALYS502
AHIS503
AHIS504
BGLN28
BTHR29

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 605
ChainResidue
AGLU251
ASER252
AILE253
BHIS136
BASN139

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 601
ChainResidue
BHIS101
BPHE129
BLEU133
BALA285
BSER286
BASN289
BTHR290
BALA293
BSER360
BASN362
BPRO436
BPHE437
BTHR442
BCYS444
BPRO445
BALA450
BGLU453
BILE488
B0GV602
BHOH701
BHOH719
BHOH761
BHOH823

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 0GV B 602
ChainResidue
BHIS101
BILE114
BILE125
BARG260
BTRP284
BALA285
BSER360
BLEU361
BGLY485
BLEU486
BHEM601
BHOH701

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SO4 B 603
ChainResidue
BASP376
BGLY377
BTYR379
BHOH732
BHOH733
BHIS65
BVAL66
BASN81
BSER84
BLEU374
BGLU375

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 604
ChainResidue
ATYR41
ACYS44
AALA45
AGLN47
BTYR41
BCYS44
BALA45
BGLN47

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 605
ChainResidue
AHIS136
AASN139
BSER252
BILE253

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 2024-06-12

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