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3MVR

Crystal Structure of cytochrome P450 2B4-H226Y in a closed conformation

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_functionarachidonic acid 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
A0070330molecular_functionaromatase activity
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006805biological_processxenobiotic metabolic process
B0008392molecular_functionarachidonic acid 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
B0070330molecular_functionaromatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AARG98
AGLN357
AILE363
AVAL367
AHIS369
ALEU392
APRO428
APHE429
ASER430
AARG434
ACYS436
AILE114
ALEU437
AGLY438
AILE441
AALA442
AHOH993
ATRP121
AARG125
AALA298
AGLY299
ATHR302
ATHR303
ATHR306

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CM5 A 601
ChainResidue
ALYS186
APHE188
APHE195
APHE202
APHE244
ALYS251
AGLU466
AASP467

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CM5 A 602
ChainResidue
ALEU43
ALEU44
AMET46
AASP47
AARG48
AGLN215

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG98
BILE114
BTRP121
BARG125
BALA298
BGLY299
BTHR302
BTHR303
BTHR306
BGLN357
BILE363
BVAL367
BHIS369
BLEU392
BPRO428
BPHE429
BSER430
BARG434
BCYS436
BGLY438
BILE441
BALA442
BHOH778

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CM5 B 603
ChainResidue
BLEU43
BLEU44
BMET46
BASP47
BGLY50
BGLN215
BVAL216

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CM5 B 604
ChainResidue
BLYS186
BPHE188
BASP192
BVAL194
BPHE195
BLEU198
BPHE244
BLYS251
BPHE296
BASP467

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
ACYS436
BCYS436

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000250|UniProtKB:P00176
ChainResidueDetails
ASER128
BSER128

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PDB entries from 2024-07-24

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