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1F26

CRYSTAL STRUCTURE OF NO COMPLEX OF THR243VAL MUTANTS OF CYTOCHROME P450NOR

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
A0102199molecular_functionnitric oxide reductase [NAD(P)H] activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
APHE86
AMET244
ASER286
AGLY344
APHE345
AGLY346
APHE347
AHIS350
ACYS352
AALA354
ANO502
AVAL87
AHOH608
AHOH612
AHOH613
AHIS94
AARG98
AILE153
ALEU236
AALA239
AGLY240
AVAL243

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO A 502
ChainResidue
AALA239
AGLY240
AVAL243
AHEM501

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AALA55
ALYS62
AMET89
AASP90
AHIS350
AHOH610
AHOH641
AHOH668
AHOH870

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FGfGDHRCIA
ChainResidueDetails
APHE345-ALA354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 473
ChainResidueDetails
AVAL243steric role
ASER286proton shuttle (general acid/base)
ACYS352activator, metal ligand
AASP393proton shuttle (general acid/base)

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PDB entries from 2025-07-30

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