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2FDW

Crystal Structure Of Human Microsomal P450 2A6 with the inhibitor (5-(Pyridin-3-yl)furan-2-yl)methanamine bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005881cellular_componentcytoplasmic microtubule
A0006629biological_processlipid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008202biological_processsteroid metabolic process
A0008389molecular_functioncoumarin 7-hydroxylase activity
A0008392molecular_functionarachidonic acid epoxygenase activity
A0009804biological_processcoumarin metabolic process
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
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0042178biological_processxenobiotic catabolic process
A0043231cellular_componentintracellular membrane-bounded organelle
A0046226biological_processcoumarin catabolic process
A0046872molecular_functionmetal ion binding
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005881cellular_componentcytoplasmic microtubule
B0006629biological_processlipid metabolic process
B0006805biological_processxenobiotic metabolic process
B0008202biological_processsteroid metabolic process
B0008389molecular_functioncoumarin 7-hydroxylase activity
B0008392molecular_functionarachidonic acid epoxygenase activity
B0009804biological_processcoumarin metabolic process
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
B0019899molecular_functionenzyme binding
B0020037molecular_functionheme binding
B0042178biological_processxenobiotic catabolic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0046226biological_processcoumarin catabolic process
B0046872molecular_functionmetal ion binding
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005881cellular_componentcytoplasmic microtubule
C0006629biological_processlipid metabolic process
C0006805biological_processxenobiotic metabolic process
C0008202biological_processsteroid metabolic process
C0008389molecular_functioncoumarin 7-hydroxylase activity
C0008392molecular_functionarachidonic acid epoxygenase activity
C0009804biological_processcoumarin metabolic process
C0016020cellular_componentmembrane
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
C0019899molecular_functionenzyme binding
C0020037molecular_functionheme binding
C0042178biological_processxenobiotic catabolic process
C0043231cellular_componentintracellular membrane-bounded organelle
C0046226biological_processcoumarin catabolic process
C0046872molecular_functionmetal ion binding
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0005881cellular_componentcytoplasmic microtubule
D0006629biological_processlipid metabolic process
D0006805biological_processxenobiotic metabolic process
D0008202biological_processsteroid metabolic process
D0008389molecular_functioncoumarin 7-hydroxylase activity
D0008392molecular_functionarachidonic acid epoxygenase activity
D0009804biological_processcoumarin metabolic process
D0016020cellular_componentmembrane
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
D0019899molecular_functionenzyme binding
D0020037molecular_functionheme binding
D0042178biological_processxenobiotic catabolic process
D0043231cellular_componentintracellular membrane-bounded organelle
D0046226biological_processcoumarin catabolic process
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AARG101
ALEU395
APRO431
APHE432
ASER433
AARG437
ACYS439
APHE440
AGLY441
AD3G501
AHOH502
AVAL117
AHOH517
AHOH520
AARG128
AGLY301
AGLY302
ATHR305
ATHR309
AGLN360
AARG372

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE D3G A 501
ChainResidue
APHE107
APHE111
APHE209
AASN297
AILE300
AGLY301
ATHR305
APHE480
AHEM500

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG101
BVAL116
BVAL117
BARG128
BGLY301
BGLY302
BTHR305
BTHR309
BARG372
BLEU395
BPRO431
BPHE432
BSER433
BARG437
BCYS439
BPHE440
BGLY441
BD3G501
BHOH506
BHOH512

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE D3G B 501
ChainResidue
BPHE107
BPHE111
BPHE118
BPHE209
BASN297
BILE300
BGLY301
BTHR305
BPHE480
BHEM500

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM C 500
ChainResidue
CARG101
CVAL117
CARG128
CGLY301
CGLY302
CTHR305
CGLN360
CARG372
CLEU395
CPRO431
CPHE432
CSER433
CARG437
CCYS439
CPHE440
CGLY441
CD3G501
CHOH525

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE D3G C 501
ChainResidue
CPHE107
CPHE111
CASN297
CILE300
CGLY301
CTHR305
CPHE480
CHEM500

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM D 500
ChainResidue
DASN438
DCYS439
DPHE440
DGLY441
DD3G501
DHOH578
DARG101
DVAL117
DARG128
DGLY301
DGLY302
DTHR305
DGLN360
DARG372
DLEU395
DPRO431
DPHE432
DSER433
DARG437

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE D3G D 501
ChainResidue
DPHE107
DPHE111
DPHE209
DASN297
DILE300
DGLY301
DTHR305
DPHE480
DHEM500

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSiGKRNCFG
ChainResidueDetails
APHE432-GLY441

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
APHE107
BPHE107
CPHE107
DPHE107

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASN297
BASN297
CASN297
DASN297

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS439
BCYS439
CCYS439
DCYS439

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PDB entries from 2024-04-24

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