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2CD8

Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)

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
A0017000biological_processantibiotic biosynthetic process
A0020037molecular_functionheme binding
A0033068biological_processmacrolide biosynthetic process
A0046872molecular_functionmetal ion binding
A0055114biological_processobsolete oxidation-reduction process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0017000biological_processantibiotic biosynthetic process
B0020037molecular_functionheme binding
B0033068biological_processmacrolide biosynthetic process
B0046872molecular_functionmetal ion binding
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 419
ChainResidue
ALYS72
ATHR248
ALEU251
AALA293
ATHR294
AARG296
AALA346
APHE347
AGLY348
AILE351
AHIS352
AMET92
ACYS354
AILE355
AGLY356
ALEU359
APXI420
AHOH2138
ALEU93
AHIS100
AARG104
APHE111
AALA243
AGLY244
ATHR247

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PXI A 420
ChainResidue
ATRP74
AGLU85
ALEU88
AASN89
ALEU93
AGLU94
APHE178
AVAL179
AVAL242
AALA243
AVAL290
ASER292
ATHR294
AHEM419
AHOH2139

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 419
ChainResidue
BMET92
BLEU93
BHIS100
BARG104
BPHE111
BLEU240
BALA243
BGLY244
BTHR247
BTHR248
BLEU251
BPRO289
BALA293
BTHR294
BARG296
BALA346
BILE351
BHIS352
BCYS354
BILE355
BGLY356
BALA360
BPXI420
BHOH2102

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PXI B 420
ChainResidue
BGLU85
BLEU88
BASN89
BLEU93
BGLU94
BPHE178
BVAL179
BMET191
BHIS238
BVAL242
BALA243
BGLU246
BVAL290
BTHR294
BILE395
BHEM419

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGIHFCIG
ChainResidueDetails
APHE347-GLY356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459
ChainResidueDetails
AGLU94
AALA187
AHIS238
BGLU94
BALA187
BHIS238

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:16825192, ECO:0000269|PubMed:19124459, ECO:0000269|PubMed:19833867, ECO:0000269|PubMed:24627965, ECO:0000312|PDB:2C6H, ECO:0000312|PDB:2C7X, ECO:0000312|PDB:2CA0, ECO:0000312|PDB:2CD8, ECO:0000312|PDB:2VZ7, ECO:0000312|PDB:2VZM, ECO:0000312|PDB:2WHW, ECO:0000312|PDB:2WI9, ECO:0000312|PDB:3ZK5, ECO:0000312|PDB:4B7D, ECO:0000312|PDB:4B7S, ECO:0000312|PDB:4BF4
ChainResidueDetails
ACYS354
BCYS354

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU246
ATHR247

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU246
BTHR247

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PDB entries from 2024-10-16

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