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6M7X

Structure of human CYP11B1 in complex with fadrozole

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004507molecular_functionsteroid 11-beta-monooxygenase activity
A0005506molecular_functioniron ion binding
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006700biological_processC21-steroid hormone biosynthetic process
A0006704biological_processglucocorticoid biosynthetic process
A0006955biological_processimmune response
A0008203biological_processcholesterol metabolic process
A0008217biological_processregulation of blood pressure
A0016125biological_processsterol metabolic process
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0032342biological_processaldosterone biosynthetic process
A0032870biological_processcellular response to hormone stimulus
A0034650biological_processcortisol metabolic process
A0034651biological_processcortisol biosynthetic process
A0035865biological_processcellular response to potassium ion
A0042593biological_processglucose homeostasis
A0046872molecular_functionmetal ion binding
A0047783molecular_functioncorticosterone 18-monooxygenase activity
A0071375biological_processcellular response to peptide hormone stimulus
A1901615biological_processorganic hydroxy compound metabolic process
B0004497molecular_functionmonooxygenase activity
B0004507molecular_functionsteroid 11-beta-monooxygenase activity
B0005506molecular_functioniron ion binding
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0006629biological_processlipid metabolic process
B0006694biological_processsteroid biosynthetic process
B0006700biological_processC21-steroid hormone biosynthetic process
B0006704biological_processglucocorticoid biosynthetic process
B0006955biological_processimmune response
B0008203biological_processcholesterol metabolic process
B0008217biological_processregulation of blood pressure
B0016125biological_processsterol metabolic process
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0032342biological_processaldosterone biosynthetic process
B0032870biological_processcellular response to hormone stimulus
B0034650biological_processcortisol metabolic process
B0034651biological_processcortisol biosynthetic process
B0035865biological_processcellular response to potassium ion
B0042593biological_processglucose homeostasis
B0046872molecular_functionmetal ion binding
B0047783molecular_functioncorticosterone 18-monooxygenase activity
B0071375biological_processcellular response to peptide hormone stimulus
B1901615biological_processorganic hydroxy compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue JD7 A 601
ChainResidue
APHE130
AGLY314
ATHR318
APHE381
APHE487
AILE488
AHEM602
AHOH734

site_idAC2
Number of Residues18
Detailsbinding site for residue HEM A 602
ChainResidue
AVAL129
APHE130
ATRP137
AARG141
ALEU311
AGLY314
ATHR319
ALEU382
AARG384
APRO442
APHE443
AGLY444
APHE445
AARG448
ACYS450
AJD7601
AHOH734
AARG110

site_idAC3
Number of Residues8
Detailsbinding site for residue JD7 B 601
ChainResidue
BPHE231
BGLY314
BPHE381
BPHE487
BILE488
BHEM602
BHOH744
BHOH818

site_idAC4
Number of Residues19
Detailsbinding site for residue HEM B 602
ChainResidue
BARG110
BVAL129
BPHE130
BTRP137
BARG141
BLEU311
BGLY314
BTHR319
BPRO322
BLEU382
BARG384
BPRO442
BPHE443
BGLY444
BPHE445
BARG448
BCYS450
BJD7601
BHOH744

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGMRQCLG
ChainResidueDetails
APHE443-GLY452

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000250|UniProtKB:P19099
ChainResidueDetails
ACYS450
BCYS450

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PDB entries from 2024-07-10

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