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5IUZ

STRUCTURE OF P450 2B4 F202W MUTANT (CYMAL-5)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006805biological_processxenobiotic metabolic process
A0008392molecular_functionarachidonate epoxygenase activity
A0016020cellular_componentmembrane
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
A0019373biological_processepoxygenase P450 pathway
A0020037molecular_functionheme binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006805biological_processxenobiotic metabolic process
B0008392molecular_functionarachidonate epoxygenase activity
B0016020cellular_componentmembrane
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016712molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
B0019373biological_processepoxygenase P450 pathway
B0020037molecular_functionheme binding
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue HEM A 501
ChainResidue
AARG98
ATHR303
ATHR306
AVAL367
AHIS369
ALEU392
APRO428
ASER430
AARG434
ACYS436
ALEU437
AVAL113
AGLY438
AALA442
AILE114
ATRP121
AARG125
AILE179
AALA298
AGLY299
ATHR302

site_idAC2
Number of Residues6
Detailsbinding site for residue CM5 A 502
ChainResidue
ALYS186
APHE188
ALEU198
APHE244
ALYS251
AASP467

site_idAC3
Number of Residues8
Detailsbinding site for residue CM5 A 503
ChainResidue
ALEU44
AMET46
AASP47
AGLY50
AVAL216
AHOH648
AHOH679
AHOH721

site_idAC4
Number of Residues20
Detailsbinding site for residue HEM B 501
ChainResidue
BARG98
BILE114
BTRP121
BARG125
BALA298
BGLY299
BTHR302
BTHR303
BTHR306
BILE363
BVAL367
BHIS369
BLEU392
BPRO428
BSER430
BARG434
BCYS436
BLEU437
BGLY438
BHOH636

site_idAC5
Number of Residues8
Detailsbinding site for residue CM5 B 502
ChainResidue
BPHE188
BPHE195
BLEU198
BPHE244
BPHE296
BASP467
BHOH601
BHOH668

site_idAC6
Number of Residues4
Detailsbinding site for residue CM5 B 503
ChainResidue
BLEU43
BMET46
BASP47
BGLY50

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSlGKRICLG
ChainResidueDetails
APHE429-GLY438

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AGLN455
BGLN455

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P00176
ChainResidueDetails
AGLN147
BGLN147

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PDB entries from 2024-11-06

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