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1GWI

The 1.92 A structure of Streptomyces coelicolor A3(2) CYP154C1: A new monooxygenase that functionalizes macrolide ring systems

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
A0042440biological_processpigment metabolic 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
B0042440biological_processpigment metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1410
ChainResidue
AHIS261
APRO262
AGLU263
AGLN264

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1411
ChainResidue
APRO384
AALA385
AHOH2250

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1412
ChainResidue
AHOH2251
AHOH2252
AHOH2253
AHOH2254
BTHR228
BALA230
AGLY89
AARG90

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1413
ChainResidue
AGLU163
AGLU164
AHOH2120
AHOH2255
AHOH2256

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 1408
ChainResidue
AHIS408
BSER179
BTHR180
BGLN181
BLYS391
BPHE400
BHOH2261
BHOH2262

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1409
ChainResidue
BHIS261
BPRO262
BGLU263
BGLN264

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1410
ChainResidue
BARG169
BLYS176

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1411
ChainResidue
BPRO384
BALA385

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 1414
ChainResidue
AMET92
AHIS100
AARG104
ALEU111
AMET239
AGLY243
ATHR246
ATHR247
ALEU250
ALEU283
AVAL292
AARG295
ATYR318
ASER347
APHE348
AGLY349
AHIS353
ACYS355
APRO356
AGLY357
ASER361
AHOH2145
AHOH2257

site_idBC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 1412
ChainResidue
BMET92
BLEU93
BHIS100
BARG104
BLEU111
BMET239
BGLY243
BTHR246
BTHR247
BLEU250
BVAL292
BARG295
BTYR318
BSER347
BPHE348
BGLY349
BHIS353
BCYS355
BPRO356
BSER361
BHOH2044
BHOH2162
BHOH2263

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGhGPHVCPG
ChainResidueDetails
APHE348-GLY357

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU245
ATHR246

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU245
BTHR246

259987

PDB entries from 2026-09-23

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