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5XW2

Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form

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
Functional Information from PDB Data
site_idAC1
Number of Residues26
Detailsbinding site for residue HEM A 401
ChainResidue
ALEU74
ALEU244
AVAL283
ATHR286
AARG288
APHE311
AGLY338
APHE339
AGLY340
AILE343
AHIS344
ALEU75
ACYS346
AGLY348
ALEU351
AHOH536
AHOH557
AHOH585
AHOH772
AHIS82
AARG86
APHE93
AMET232
AALA236
AGLY237
ATHR240

site_idAC2
Number of Residues10
Detailsbinding site for residue GOL A 402
ChainResidue
AGLU111
AGLU274
AASN334
APRO335
AHIS336
APHE339
AARG341
AARG353
AHOH621
AHOH721

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 403
ChainResidue
AHIS91
AASP206
ALEU207

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 404
ChainResidue
AMET32
AASN33
AHOH555
AHOH620

site_idAC5
Number of Residues3
Detailsbinding site for residue MG A 405
ChainResidue
AARG59
ATHR290
AASP304

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

227344

PDB entries from 2024-11-13

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