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1SE6

Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase activity
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
A0042440biological_processpigment metabolic process
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0006707biological_processcholesterol catabolic process
B0008395molecular_functionsteroid hydroxylase activity
B0016491molecular_functionoxidoreductase activity
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0020037molecular_functionheme binding
B0036199molecular_functioncholest-4-en-3-one 26-monooxygenase activity
B0042440biological_processpigment metabolic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SPK A 631
ChainResidue
AGLY376
ALYS378
AALA380
AHIS405
BLYS378
BTHR403

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 430
ChainResidue
AHIS101
AARG105
ALEU239
AGLY242
AALA245
ALEU282
AHIS287
AARG295
ATYR318
ASER345
APHE346
AHIS351
ACYS353
APRO354
AALA359
AHOH694
AHOH771
AARG71
AVAL93
AGLY94

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM B 430
ChainResidue
BARG71
BVAL93
BGLY94
BHIS101
BARG105
BPHE112
BLEU239
BGLY242
BALA245
BASN249
BHIS287
BARG295
BTYR318
BSER345
BPHE346
BHIS351
BCYS353
BPRO354
BHOH445
BHOH495
BHOH534

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MES A 632
ChainResidue
AASP15
ATRP16
APRO17
ASER43
ALEU44
APRO45
AHOH670

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGPHYCPG
ChainResidueDetails
APHE346-GLY355

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15659395, ECO:0000269|PubMed:16239228, ECO:0007744|PDB:1T93, ECO:0007744|PDB:2D09
ChainResidueDetails
AARG288
ALEU293
BARG288
BLEU293

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:15659395, ECO:0000269|PubMed:16239228, ECO:0000269|PubMed:22203090, ECO:0007744|PDB:1S1F, ECO:0007744|PDB:1SE6, ECO:0007744|PDB:1T93, ECO:0007744|PDB:2D09, ECO:0007744|PDB:2D0E, ECO:0007744|PDB:3TZO
ChainResidueDetails
ACYS353
BCYS353

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Involved in determining product regiospecificity => ECO:0000269|PubMed:22203090
ChainResidueDetails
AILE87
BILE87

218853

PDB entries from 2024-04-24

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