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1F4U

THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0004601molecular_functionperoxidase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
B0004497molecular_functionmonooxygenase activity
B0004601molecular_functionperoxidase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
B0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 369
ChainResidue
BGLY156
BLYS157
BARG256
BVAL258
BARG279

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 369
ChainResidue
AGLY156
ALYS157
AARG256
AARG279

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 410
ChainResidue
AMET68
ALEU69
AHIS76
AARG80
ALEU206
AGLY210
ATHR213
ATHR214
ALEU217
APRO253
ATHR257
AARG259
ASER309
APHE310
AGLY311
AHIS315
ACYS317
AIMD411

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD A 411
ChainResidue
APHE153
AALA209
ATHR213
AHEM410

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 410
ChainResidue
BMET68
BLEU69
BHIS76
BARG80
BLEU206
BGLY210
BTHR213
BTHR214
BLEU217
BPRO253
BTHR257
BARG259
BSER309
BPHE310
BGLY311
BHIS315
BCYS317
BIMD411

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IMD B 411
ChainResidue
BPHE153
BALA209
BTHR213
BHEM410

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGsGIHLCLG
ChainResidueDetails
APHE310-GLY319

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:10859321, ECO:0000269|PubMed:10957637
ChainResidueDetails
AHIS76
BHIS315
AARG80
ATHR257
AARG259
AHIS315
BHIS76
BARG80
BTHR257
BARG259

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS317
BCYS317

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU212
ATHR213

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU212
BTHR213

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PDB entries from 2025-06-11

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