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6WR1

Human steroidogenic cytochrome P450 17A1 mutant N52Y with inhibitor abiraterone

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004508molecular_functionsteroid 17-alpha-monooxygenase activity
A0005506molecular_functioniron ion binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006702biological_processandrogen biosynthetic process
A0006704biological_processglucocorticoid biosynthetic process
A0007548biological_processsex differentiation
A0008202biological_processsteroid metabolic process
A0008395molecular_functionsteroid hydroxylase activity
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
A0016829molecular_functionlyase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0030424cellular_componentaxon
A0034651biological_processcortisol biosynthetic process
A0042445biological_processhormone metabolic process
A0042446biological_processhormone biosynthetic process
A0042448biological_processprogesterone metabolic process
A0043025cellular_componentneuronal cell body
A0046872molecular_functionmetal ion binding
A0120254biological_processolefinic compound metabolic process
B0004497molecular_functionmonooxygenase activity
B0004508molecular_functionsteroid 17-alpha-monooxygenase activity
B0005506molecular_functioniron ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006694biological_processsteroid biosynthetic process
B0006702biological_processandrogen biosynthetic process
B0006704biological_processglucocorticoid biosynthetic process
B0007548biological_processsex differentiation
B0008202biological_processsteroid metabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016712molecular_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
B0016829molecular_functionlyase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030424cellular_componentaxon
B0034651biological_processcortisol biosynthetic process
B0042445biological_processhormone metabolic process
B0042446biological_processhormone biosynthetic process
B0042448biological_processprogesterone metabolic process
B0043025cellular_componentneuronal cell body
B0046872molecular_functionmetal ion binding
B0120254biological_processolefinic compound metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue HEM A 600
ChainResidue
AARG96
ALEU370
AILE371
AHIS373
APRO434
APHE435
AARG440
ACYS442
AILE443
AGLY444
ALEU447
AILE112
AALA448
AAER601
AHOH748
AALA113
ATRP121
AARG125
AALA302
AGLY303
ATHR306
AVAL366

site_idAC2
Number of Residues8
Detailsbinding site for residue AER A 601
ChainResidue
AALA113
ATYR201
AASN202
AILE205
AGLY297
ATHR306
AVAL482
AHEM600

site_idAC3
Number of Residues20
Detailsbinding site for residue HEM B 600
ChainResidue
BARG96
BILE112
BALA113
BTRP121
BARG125
BALA302
BGLY303
BTHR306
BVAL366
BLEU370
BILE371
BHIS373
BPRO434
BPHE435
BARG440
BCYS442
BGLY444
BALA448
BAER601
BHOH742

site_idAC4
Number of Residues7
Detailsbinding site for residue AER B 601
ChainResidue
BALA113
BPHE114
BTYR201
BASN202
BILE205
BTHR306
BHEM600

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGaGPRSCIG
ChainResidueDetails
APHE435-GLY444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25301938","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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