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3ME6

Crystal structure of cytochrome 2B4 in complex with the anti-platelet drug clopidogrel

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0006082biological_processorganic acid metabolic process
A0006805biological_processxenobiotic metabolic process
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
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005789cellular_componentendoplasmic reticulum membrane
B0006082biological_processorganic acid metabolic process
B0006805biological_processxenobiotic metabolic process
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
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0005737cellular_componentcytoplasm
C0005789cellular_componentendoplasmic reticulum membrane
C0006082biological_processorganic acid metabolic process
C0006805biological_processxenobiotic metabolic process
C0008392molecular_functionarachidonate epoxygenase activity
C0016491molecular_functionoxidoreductase activity
C0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
C0016712molecular_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
C0019373biological_processepoxygenase P450 pathway
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0005737cellular_componentcytoplasm
D0005789cellular_componentendoplasmic reticulum membrane
D0006082biological_processorganic acid metabolic process
D0006805biological_processxenobiotic metabolic process
D0008392molecular_functionarachidonate epoxygenase activity
D0016491molecular_functionoxidoreductase activity
D0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
D0016712molecular_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
D0019373biological_processepoxygenase P450 pathway
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AARG98
AHIS369
ALEU392
APHE429
ASER430
AARG434
ACYS436
AGLY438
AALA442
ACGE501
AILE114
ATRP121
AARG125
AALA298
AGLY299
ATHR303
AILE363
AVAL367

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CGE A 501
ChainResidue
APHE206
AILE209
APHE297
AALA298
ATHR302
AVAL367
AVAL477
AHEM500

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG98
BILE114
BTRP121
BARG125
BALA298
BGLY299
BTHR302
BTHR303
BGLN357
BILE363
BVAL367
BHIS369
BLEU392
BPRO428
BPHE429
BSER430
BARG434
BCYS436
BALA442
BCGE501

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CGE B 501
ChainResidue
BPHE206
BILE209
BPHE297
BALA298
BTHR302
BVAL477
BHEM500

site_idAC5
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM C 500
ChainResidue
CARG98
CILE114
CTRP121
CARG125
CALA298
CGLY299
CTHR302
CTHR303
CILE363
CVAL367
CHIS369
CLEU392
CPRO428
CPHE429
CSER430
CARG434
CCYS436
CGLY438
CALA442
CCGE501

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CGE C 501
ChainResidue
CPHE206
CILE209
CPHE297
CALA298
CTHR302
CVAL367
CVAL477
CHEM500

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM D 500
ChainResidue
DCGE501
DARG98
DILE114
DTRP121
DARG125
DALA298
DGLY299
DTHR303
DTHR306
DILE363
DVAL367
DHIS369
DLEU392
DPRO428
DPHE429
DSER430
DARG434
DCYS436
DALA442

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CGE D 501
ChainResidue
DPHE206
DILE209
DPHE297
DALA298
DTHR302
DVAL367
DVAL477
DHEM500

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 Residues4
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P00176","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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