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3UA5

Crystal Structure of P450 2B6 (Y226H/K262R) in complex with two molecules of Amlodipine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
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
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
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
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 Residues16
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AARG98
APHE429
ASER430
AARG434
ACYS436
ALEU437
AGLY438
A06X501
AVAL113
ATRP121
AARG125
AALA298
AGLY299
ATHR302
AHIS369
APRO428

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 06X A 501
ChainResidue
AILE101
APHE115
AALA298
ATHR300
ATHR302
AVAL477
AHEM500

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 06X A 502
ChainResidue
AARG49
ALEU51
AARG73
AGLN215
AGLU218
ALEU219
AMET365
APHE389
AGLY476
AVAL477

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG98
BVAL113
BTRP121
BARG125
BTHR302
BTHR306
BLEU362
BHIS369
BPRO428
BPHE429
BSER430
BARG434
BCYS436
BLEU437
BGLY438
B06X501

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 06X B 501
ChainResidue
BILE101
BPHE115
BPHE206
BSER210
BPHE297
BALA298
BTHR300
BGLU301
BTHR302
BVAL477
BHEM500

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 06X B 502
ChainResidue
BLEU51
BARG73
BGLN215
BGLU218
BLEU219
BPRO368
BPHE389
BGLY476
BVAL477

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 site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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