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5L94

The 2.25 A crystal structure of CYP109E1 from Bacillus megaterium in complex with testosterone

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0006707biological_processcholesterol catabolic process
A0008395molecular_functionsteroid hydroxylase 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
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0006707biological_processcholesterol catabolic process
B0008395molecular_functionsteroid hydroxylase 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
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue HEM A 501
ChainResidue
ALEU84
AALA344
APHE345
AGLY346
AHIS350
ACYS352
AGLY354
AALA358
ATES502
AHOH612
AHOH682
AILE85
AHIS92
AARG96
AILE147
ALEU238
AALA242
ATHR246
AARG294

site_idAC2
Number of Residues4
Detailsbinding site for residue TES A 502
ChainResidue
AILE241
AVAL289
APHE391
AHEM501

site_idAC3
Number of Residues22
Detailsbinding site for residue HEM B 501
ChainResidue
BLEU84
BILE85
BHIS92
BARG96
BILE147
BALA242
BGLY243
BTHR246
BTHR247
BLEU292
BARG294
BALA344
BPHE345
BGLY346
BILE349
BHIS350
BCYS352
BGLY354
BALA358
BHOH624
BHOH638
BHOH678

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGIHFCLG
ChainResidueDetails
APHE345-GLY354

219140

PDB entries from 2024-05-01

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