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6MA7

Human CYP3A4 bound to an inhibitor fluconazole

Functional Information from GO Data
ChainGOidnamespacecontents
A0002933biological_processlipid hydroxylation
A0004497molecular_functionmonooxygenase activity
A0005496molecular_functionsteroid binding
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006706biological_processsteroid catabolic process
A0006805biological_processxenobiotic metabolic process
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008209biological_processandrogen metabolic process
A0008210biological_processestrogen metabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0008401molecular_functionretinoic acid 4-hydroxylase activity
A0009822biological_processalkaloid catabolic process
A0016020cellular_componentmembrane
A0016098biological_processmonoterpenoid metabolic process
A0016491molecular_functionoxidoreductase activity
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
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0030343molecular_functionvitamin D3 25-hydroxylase activity
A0034875molecular_functioncaffeine oxidase activity
A0036378biological_processcalcitriol biosynthetic process from calciol
A0042178biological_processxenobiotic catabolic process
A0042359biological_processvitamin D metabolic process
A0042369biological_processvitamin D catabolic process
A0042572biological_processretinol metabolic process
A0042573biological_processretinoic acid metabolic process
A0042759biological_processlong-chain fatty acid biosynthetic process
A0043231cellular_componentintracellular membrane-bounded organelle
A0046222biological_processaflatoxin metabolic process
A0046872molecular_functionmetal ion binding
A0050591molecular_functionquinine 3-monooxygenase activity
A0050649molecular_functiontestosterone 6-beta-hydroxylase activity
A0062181molecular_function1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity
A0062187molecular_functionanandamide 8,9 epoxidase activity
A0062188molecular_functionanandamide 11,12 epoxidase activity
A0062189molecular_functionanandamide 14,15 epoxidase activity
A0070576molecular_functionvitamin D 24-hydroxylase activity
A0070989biological_processoxidative demethylation
A0101020molecular_functionestrogen 16-alpha-hydroxylase activity
A0101021molecular_functionestrogen 2-hydroxylase activity
A0102320molecular_function1,8-cineole 2-exo-monooxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue HEM A 601
ChainResidue
AARG105
AALA370
AARG375
APRO434
APHE435
AGLY436
ASER437
AARG440
AASN441
ACYS442
AILE443
AILE118
AGLY444
ATPF602
AHOH751
ASER119
ATRP126
AARG130
APHE137
APHE302
AALA305
AGLY306

site_idAC2
Number of Residues9
Detailsbinding site for residue TPF A 602
ChainResidue
AARG105
AARG212
AALA305
AILE369
AALA370
AHEM601
ADMS603
AHOH736
AHOH760

site_idAC3
Number of Residues3
Detailsbinding site for residue DMS A 603
ChainResidue
ASER119
APHE304
ATPF602

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 604
ChainResidue
AGLY177
AALA178
AMET181
ASER195
AVAL204
ATYR307

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 Residues1
DetailsBINDING: axial binding residue => ECO:0007744|PDB:1TQN, ECO:0007744|PDB:1W0G
ChainResidueDetails
ACYS442

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PDB entries from 2024-11-06

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