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4NKX

Human steroidogenic cytochrome P450 17A1 mutant A105L with substrate progesterone

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
A0006694biological_processsteroid biosynthetic process
A0006702biological_processandrogen biosynthetic process
A0006704biological_processglucocorticoid biosynthetic process
A0007548biological_processsex differentiation
A0008202biological_processsteroid metabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016020cellular_componentmembrane
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016829molecular_functionlyase activity
A0019825molecular_functionoxygen binding
A0020037molecular_functionheme binding
A0030424cellular_componentaxon
A0042445biological_processhormone metabolic process
A0042446biological_processhormone biosynthetic process
A0042448biological_processprogesterone metabolic process
A0043025cellular_componentneuronal cell body
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0004508molecular_functionsteroid 17-alpha-monooxygenase activity
B0005506molecular_functioniron ion binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006694biological_processsteroid biosynthetic process
B0006702biological_processandrogen biosynthetic process
B0006704biological_processglucocorticoid biosynthetic process
B0007548biological_processsex differentiation
B0008202biological_processsteroid metabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0016020cellular_componentmembrane
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016829molecular_functionlyase activity
B0019825molecular_functionoxygen binding
B0020037molecular_functionheme binding
B0030424cellular_componentaxon
B0042445biological_processhormone metabolic process
B0042446biological_processhormone biosynthetic process
B0042448biological_processprogesterone metabolic process
B0043025cellular_componentneuronal cell body
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0004508molecular_functionsteroid 17-alpha-monooxygenase activity
C0005506molecular_functioniron ion binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006694biological_processsteroid biosynthetic process
C0006702biological_processandrogen biosynthetic process
C0006704biological_processglucocorticoid biosynthetic process
C0007548biological_processsex differentiation
C0008202biological_processsteroid metabolic process
C0008395molecular_functionsteroid hydroxylase activity
C0016020cellular_componentmembrane
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0016829molecular_functionlyase activity
C0019825molecular_functionoxygen binding
C0020037molecular_functionheme binding
C0030424cellular_componentaxon
C0042445biological_processhormone metabolic process
C0042446biological_processhormone biosynthetic process
C0042448biological_processprogesterone metabolic process
C0043025cellular_componentneuronal cell body
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0004508molecular_functionsteroid 17-alpha-monooxygenase activity
D0005506molecular_functioniron ion binding
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006694biological_processsteroid biosynthetic process
D0006702biological_processandrogen biosynthetic process
D0006704biological_processglucocorticoid biosynthetic process
D0007548biological_processsex differentiation
D0008202biological_processsteroid metabolic process
D0008395molecular_functionsteroid hydroxylase activity
D0016020cellular_componentmembrane
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0016829molecular_functionlyase activity
D0019825molecular_functionoxygen binding
D0020037molecular_functionheme binding
D0030424cellular_componentaxon
D0042445biological_processhormone metabolic process
D0042446biological_processhormone biosynthetic process
D0042448biological_processprogesterone metabolic process
D0043025cellular_componentneuronal cell body
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 600
ChainResidue
AARG96
AVAL366
AILE371
AHIS373
APRO434
APHE435
AARG440
ASER441
ACYS442
AGLY444
AILE112
AALA113
ATRP121
AARG125
AILE299
AALA302
ATHR306
AVAL310

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE STR A 601
ChainResidue
AALA113
APHE114
AASN202
AILE205
AASP298
AGLY301
AGLU305
ATHR306
AILE371
AVAL483

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 600
ChainResidue
BARG96
BILE112
BALA113
BTRP121
BARG125
BALA302
BGLY303
BTHR306
BVAL310
BVAL366
BLEU370
BILE371
BHIS373
BPRO434
BPHE435
BARG440
BCYS442
BALA448

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE STR B 601
ChainResidue
BALA113
BASN202
BASP298
BTHR306
BILE371
BVAL483

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM C 600
ChainResidue
CARG96
CILE112
CALA113
CTRP121
CARG125
CILE299
CALA302
CGLY303
CTHR306
CTHR307
CVAL366
CLEU370
CILE371
CHIS373
CPRO434
CPHE435
CARG440
CCYS442
CILE443
CALA448
CSTR601

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE STR C 601
ChainResidue
CALA113
CASN202
CILE205
CASP298
CVAL366
CILE371
CVAL483
CHEM600

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM D 600
ChainResidue
DALA448
DSTR601
DARG96
DILE112
DALA113
DTRP121
DARG125
DALA302
DGLY303
DTHR306
DVAL310
DVAL366
DLEU370
DHIS373
DPRO434
DPHE435
DARG440
DCYS442
DILE443
DGLY444

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE STR D 601
ChainResidue
DALA113
DASN202
DILE205
DASP298
DTHR306
DVAL366
DILE371
DVAL483
DHEM600

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 Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:25301938
ChainResidueDetails
AASN202
BASN202
CASN202
DASN202

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS442
BCYS442
CCYS442
DCYS442

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PDB entries from 2024-10-30

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