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4GGV

Crystal Structure of HmtT Involved in Himastatin Biosynthesis

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
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
AMET74
ATHR244
ASER283
ALEU286
AARG288
AGLY338
APHE339
AGLY340
AILE343
AHIS344
ACYS346
ASER75
ALEU347
AGLY348
AHOH501
AHOH514
AHIS82
AARG86
AILE137
ALEU233
ATHR236
AGLY237
ATHR240

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGrGIHFCLG
ChainResidueDetails
APHE339-GLY348

218853

数据于2024-04-24公开中

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