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1GED

A positive charge route for the access of nadh to heme formed in the distal heme pocket 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 Residues5
DetailsBINDING SITE FOR RESIDUE BR A 404
ChainResidue
ALEU146
ASER150
ATHR168
AASN171
AASN241

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BR A 405
ChainResidue
AASN315
AHEM501
ASER286
AALA287
ALEU288
AALA289

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
APHE86
AVAL87
AHIS94
AARG98
APHE105
ALEU236
AALA239
AGLY240
ATHR243
AMET244
AMET247
ASER286
AILE290
AGLY344
APHE345
AGLY346
APHE347
AHIS350
ACYS352
AILE353
AALA354
ABR405
AHOH502
AHOH513
AHOH527
AHOH535

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
ACYS352

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:9010754
ChainResidueDetails
AALA2

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AALA242
ATHR243

site_idMCSA1
Number of Residues4
DetailsM-CSA 473
ChainResidueDetails
ATHR243steric role
ASER286proton shuttle (general acid/base)
ACYS352activator, metal ligand
AASP393proton shuttle (general acid/base)

229183

PDB entries from 2024-12-18

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