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4RQL

Crystal structure of a human cytochrome P450 2B6 (Y226H/K262R) in complex with a monoterpene - sabinene

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008202biological_processsteroid metabolic process
A0008390molecular_functiontestosterone 16-alpha-hydroxylase activity
A0008392molecular_functionarachidonate epoxygenase activity
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
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
A0042178biological_processxenobiotic catabolic process
A0042180biological_processketone metabolic process
A0046872molecular_functionmetal ion binding
A0062184molecular_functiontestosterone 16-beta-hydroxylase activity
A0062187molecular_functionanandamide 8,9 epoxidase activity
A0062188molecular_functionanandamide 11,12 epoxidase activity
A0062189molecular_functionanandamide 14,15 epoxidase activity
A0101021molecular_functionestrogen 2-hydroxylase activity
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006805biological_processxenobiotic metabolic process
B0008202biological_processsteroid metabolic process
B0008390molecular_functiontestosterone 16-alpha-hydroxylase activity
B0008392molecular_functionarachidonate epoxygenase activity
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
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
B0042178biological_processxenobiotic catabolic process
B0042180biological_processketone metabolic process
B0046872molecular_functionmetal ion binding
B0062184molecular_functiontestosterone 16-beta-hydroxylase activity
B0062187molecular_functionanandamide 8,9 epoxidase activity
B0062188molecular_functionanandamide 11,12 epoxidase activity
B0062189molecular_functionanandamide 14,15 epoxidase activity
B0101021molecular_functionestrogen 2-hydroxylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 501
ChainResidue
AARG98
ALEU362
AVAL367
AHIS369
ALEU392
APRO428
APHE429
ASER430
AARG434
ACYS436
ALEU437
AVAL113
AGLY438
AALA442
AHOH688
AILE114
ATRP121
AARG125
AALA298
ATHR302
ATHR306
AGLN357

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CM5 A 502
ChainResidue
APHE220
APHE223

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CM5 A 503
ChainResidue
AGLU194
APHE195
ATYR244
APHE296
AHOH745

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CM5 A 504
ChainResidue
AMET46
AARG48

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SNE A 505
ChainResidue
APHE297
AALA298
ATHR302

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 506
ChainResidue
AGLU218
AMET365
APRO368
AVAL477

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM B 501
ChainResidue
BARG98
BVAL113
BILE114
BTRP121
BARG125
BMET132
BILE179
BALA298
BGLY299
BTHR302
BTHR306
BGLN357
BLEU362
BLEU363
BHIS369
BLEU392
BPRO428
BPHE429
BSER430
BARG434
BCYS436
BLEU437
BGLY438
BALA442
BHOH745

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SNE B 502
ChainResidue
BPHE297
BTHR302

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CM5 B 503
ChainResidue
BGLU194
BMET198
BPHE202
BTYR244
BHIS247
BPHE296

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CM5 B 504
ChainResidue
BMET46
BARG48
BGLY50

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CM5 B 505
ChainResidue
BPHE223

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 506
ChainResidue
BGLU218
BMET365
BPRO368
BHOH778

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
ChainResidueDetails
AGLN147
BGLN147

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PDB entries from 2025-06-18

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