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Crystal Structure of a Cytochrome P450 from the Thermoacidophilic Archaeon Picrophilus Torridus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
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
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
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
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0016712molecular_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
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 900
ChainResidue
AASP99
APHE325
ALYS326

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 910
ChainResidue
APHE280
AASP281
AARG290

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 920
ChainResidue
AILE54
ASER55
ALYS189

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 910
ChainResidue
CPHE280
CASP281
CARG290
CARG291
CHOH931

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 410
ChainResidue
APHE56
AILE57
AHIS64
AARG68
ALEU194
AGLY197
AGLY198
ATHR201
AILE241
AARG247
ALEU270
AALA296
APHE297
AGLY298
AILE301
AHIS302
ACYS304
AGLY306
AHOH944
AHOH946

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 410
ChainResidue
BPHE56
BILE57
BHIS64
BARG68
BPHE75
BLEU193
BLEU194
BGLY197
BGLY198
BTHR201
BHIS246
BARG247
BLEU270
BALA296
BPHE297
BGLY298
BILE301
BHIS302
BCYS304
BGLY306
BLEU309
BALA310
BHOH412
BHOH419
BHOH420

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM C 410
ChainResidue
CPHE56
CILE57
CHIS64
CARG68
CLEU194
CGLY197
CGLY198
CTHR201
CLEU205
CLEU235
CLEU244
CARG247
CALA296
CPHE297
CGLY298
CILE301
CHIS302
CCYS304
CGLY306

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGiGIHMCLG
ChainResidueDetails
APHE297-GLY306

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
ATHR201
AGLU200

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BTHR201
BGLU200

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
CTHR201
CGLU200

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PDB entries from 2024-11-06

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