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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
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A1410
ChainResidue
AHIS261
APRO262
AGLU263
AGLN264

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A1411
ChainResidue
APRO384
AALA385
AHOH2250

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A1412
ChainResidue
AHOH2251
AHOH2252
AHOH2253
AHOH2254
BTHR228
BALA230
AGLY89
AARG90

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1413
ChainResidue
AGLU163
AGLU164
AHOH2120
AHOH2255
AHOH2256

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B1408
ChainResidue
AHIS408
BSER179
BTHR180
BGLN181
BLYS391
BPHE400
BHOH2261
BHOH2262

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B1409
ChainResidue
BHIS261
BPRO262
BGLU263
BGLN264

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B1410
ChainResidue
BARG169
BLYS176

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B1411
ChainResidue
BPRO384
BALA385

site_idAC9
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A1414
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 B1412
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

226707

PDB entries from 2024-10-30

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