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6FSH

Crystal structure of hybrid P450 OxyBtei(BC/FGvan)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016757molecular_functionglycosyltransferase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016757molecular_functionglycosyltransferase activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0016757molecular_functionglycosyltransferase activity
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0005515molecular_functionprotein binding
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0016757molecular_functionglycosyltransferase activity
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue HEM A 401
ChainResidue
ALEU88
ATHR287
AARG289
ALEU312
AALA339
APHE340
AGLY341
AHIS345
ACYS347
AGLY349
ATHR353
AHIS96
AARG100
ALEU152
AALA236
AGLY237
AASN240
AMET244
APRO286

site_idAC2
Number of Residues6
Detailsbinding site for residue K A 402
ChainResidue
ATYR284
AARG383
ATHR384
ASER385
ATHR386
AALA388

site_idAC3
Number of Residues3
Detailsbinding site for residue K A 403
ChainResidue
ALEU235
AASP238
AASP239

site_idAC4
Number of Residues23
Detailsbinding site for residue HEM B 401
ChainResidue
BLEU88
BMET89
BHIS96
BARG100
BLEU152
BLEU155
BALA236
BGLY237
BASN240
BMET244
BPRO283
BPRO286
BTHR287
BARG289
BALA339
BPHE340
BGLY341
BILE344
BHIS345
BCYS347
BGLY349
BTHR353
BHOH521

site_idAC5
Number of Residues4
Detailsbinding site for residue K B 402
ChainResidue
APRO376
BARG100
BHIS346
BCYS347

site_idAC6
Number of Residues22
Detailsbinding site for residue HEM C 401
ChainResidue
CLEU88
CMET89
CHIS96
CARG100
CLEU152
CLEU155
CALA236
CGLY237
CASN240
CMET244
CPRO283
CPRO286
CTHR287
CARG289
CALA339
CPHE340
CGLY341
CHIS345
CCYS347
CGLY349
CTHR353
CHOH521

site_idAC7
Number of Residues23
Detailsbinding site for residue HEM D 401
ChainResidue
DHOH519
DLEU88
DMET89
DHIS96
DARG100
DLEU152
DLEU155
DALA236
DGLY237
DASN240
DVAL241
DMET244
DPRO283
DPRO286
DTHR287
DARG289
DALA339
DPHE340
DGLY341
DHIS345
DCYS347
DGLY349
DTHR353

site_idAC8
Number of Residues3
Detailsbinding site for residue ACT D 402
ChainResidue
CPRO136
DHIS337
DHIS342

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHHCLG
ChainResidueDetails
APHE340-GLY349

site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ETTWLAAGHAV
ChainResidueDetails
AGLU40-VAL50

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PDB entries from 2024-07-17

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