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1F25

CRYSTAL STRUCTURE OF NO COMPLEX OF THR243ASN MUTANTS OF CYTOCHROME P450NOR

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
A0102199molecular_functionnitric oxide reductase (NAD(P)H) activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
APHE86
AMET247
AGLY344
APHE345
AGLY346
APHE347
AHIS350
ACYS352
AALA354
ANO502
AHOH603
AVAL87
AHOH612
AHOH616
AHIS94
AARG98
AILE153
ALEU236
AALA239
AGLY240
AASN243

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO A 502
ChainResidue
AALA239
AGLY240
AASN243
AHEM501
AHOH674
AHOH892

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
AALA55
AGLU58
AMET89
AASP90
AHIS350
AHOH607
AHOH631
AHOH663
AHOH1166

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: axial binding residue
ChainResidueDetails
AILE353

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:9010754
ChainResidueDetails
ASER3

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 473
ChainResidueDetails
AMET244steric role
AALA287proton shuttle (general acid/base)
AILE353activator, metal ligand
AVAL394proton shuttle (general acid/base)

226707

PDB entries from 2024-10-30

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