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3ZK5

PikC D50N mutant bound to the 10-DML analog with the 3-(N,N-dimethylamino)ethanoate anchoring group

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 1407
ChainResidue
AMET92
ATHR248
ALEU251
APRO289
AALA293
ATHR294
AARG296
AALA346
APHE347
AGLY348
AILE351
ALEU93
AHIS352
ACYS354
AILE355
AGLY356
AALA360
AHOH2258
AHIS100
AARG104
APHE111
AILE157
AALA243
AGLY244
ATHR247

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE Z18 A 1408
ChainResidue
ALEU81
AGLU85
AGLU94
APHE178
AVAL179
AHIS238
AILE239
AVAL242
AALA243
ATHR294

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 1407
ChainResidue
BLYS72
BMET92
BLEU93
BHIS100
BARG104
BLEU240
BALA243
BGLY244
BTHR247
BTHR248
BLEU251
BPRO289
BALA293
BTHR294
BARG296
BALA346
BPHE347
BGLY348
BILE351
BHIS352
BCYS354
BILE355
BGLY356
BALA360
BHOH2231

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE Z18 B 1408
ChainResidue
BGLU85
BLEU93
BGLU94
BPHE178
BVAL179
BHIS238
BILE239
BALA243
BTHR294
BMET394
BILE395
BHOH2141

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

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PDB entries from 2024-07-17

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