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1EHE

CRYSTAL STRUCTURES OF CYTOCHROME P450NOR AND ITS MUTANTS (SER286 VAL, THR) IN THE FERRIC RESTING STATE AT CRYOGENIC TEMPERATURE: A COMPARATIVE ANALYSIS WITH MONOOXYGENASE CYTOCHROME P450S

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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
APHE86
ATHR243
AMET244
AGLY344
APHE345
AGLY346
APHE347
AHIS350
ACYS352
AILE353
AALA354
AVAL87
AALA358
AHOH502
AHOH509
AHOH519
AHOH541
AHIS94
AARG98
APHE105
AILE153
ALEU236
AALA239
AGLY240

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AALA242
ATHR243

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

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PDB entries from 2024-09-18

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