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4E2P

Crystal Structure of a Post-tailoring Hydroxylase (HmtN) Involved in the Himastatin Biosynthesis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
ALEU74
ATHR241
ALEU244
APRO282
AVAL283
ATHR286
AARG288
APHE311
AGLY338
APHE339
AHIS344
ALEU75
ACYS346
AGLY348
AHOH523
AHOH553
AHOH686
AHIS82
AARG86
AVAL137
AMET232
AALA236
AGLY237
ATHR240

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AHIS56
ASER58
ATHR70

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 404
ChainResidue
ATYR255
AGLU257
AGLN258
AHOH612

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A 405
ChainResidue
AHOH642

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

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PDB entries from 2025-10-29

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