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2BVJ

Ligand-free structure of 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
A0020037molecular_functionheme binding
A0033068biological_processmacrolide biosynthetic process
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
B0020037molecular_functionheme binding
B0033068biological_processmacrolide biosynthetic process
B0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 1408
ChainResidue
ALYS72
ATHR248
ALEU251
APRO289
AALA293
ATHR294
AARG296
AALA346
APHE347
AGLY348
AILE351
AMET92
AHIS352
ACYS354
AILE355
AGLY356
AALA360
AHOH2087
AHOH2144
ALEU93
AHIS100
AARG104
APHE111
AALA243
AGLY244
ATHR247

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 1409
ChainResidue
ALEU135
AARG374
ACYS375
ATRP405
AHOH2143

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DTT A 1410
ChainResidue
AARG120
AASP277
AARG365
AARG369
AHOH2098
BGLY21
BGLN22

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 1408
ChainResidue
BLYS72
BMET92
BLEU93
BHIS100
BARG104
BPHE111
BLEU240
BALA243
BGLY244
BTHR247
BTHR248
BLEU251
BALA293
BTHR294
BARG296
BALA346
BPHE347
BGLY348
BHIS352
BCYS354
BILE355
BALA360
BHOH2101
BHOH2140

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME B 1409
ChainResidue
BLEU135
BARG374
BCYS375
BTRP405
BHOH2168
BHOH2169

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 Residues26
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"16825192","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19124459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19833867","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24627965","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2C6H","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2C7X","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CA0","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2CD8","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZ7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2VZM","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WHW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"2WI9","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"3ZK5","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7D","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4B7S","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4BF4","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

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 2026-09-30

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