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2PG6

Crystal Structure of Human Microsomal P450 2A6 L240C/N297Q

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
A0008389molecular_functioncoumarin 7-hydroxylase activity
A0008392molecular_functionarachidonic acid epoxygenase activity
A0009804biological_processcoumarin metabolic process
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
A0046222biological_processaflatoxin metabolic process
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
B0008389molecular_functioncoumarin 7-hydroxylase activity
B0008392molecular_functionarachidonic acid epoxygenase activity
B0009804biological_processcoumarin metabolic process
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
B0046222biological_processaflatoxin metabolic process
B0046872molecular_functionmetal ion binding
B0070330molecular_functionaromatase activity
C0004497molecular_functionmonooxygenase activity
C0005506molecular_functioniron ion binding
C0005737cellular_componentcytoplasm
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006805biological_processxenobiotic metabolic process
C0008389molecular_functioncoumarin 7-hydroxylase activity
C0008392molecular_functionarachidonic acid epoxygenase activity
C0009804biological_processcoumarin metabolic process
C0016020cellular_componentmembrane
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
C0043231cellular_componentintracellular membrane-bounded organelle
C0046222biological_processaflatoxin metabolic process
C0046872molecular_functionmetal ion binding
C0070330molecular_functionaromatase activity
D0004497molecular_functionmonooxygenase activity
D0005506molecular_functioniron ion binding
D0005737cellular_componentcytoplasm
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006805biological_processxenobiotic metabolic process
D0008389molecular_functioncoumarin 7-hydroxylase activity
D0008392molecular_functionarachidonic acid epoxygenase activity
D0009804biological_processcoumarin metabolic process
D0016020cellular_componentmembrane
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
D0043231cellular_componentintracellular membrane-bounded organelle
D0046222biological_processaflatoxin metabolic process
D0046872molecular_functionmetal ion binding
D0070330molecular_functionaromatase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AARG101
APRO431
APHE432
ASER433
AARG437
ACYS439
APHE440
AGLY441
AHOH514
AHOH516
AVAL116
AVAL117
AARG128
AGLY302
ATHR305
ATHR309
AGLN360
AARG372

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG101
BVAL117
BARG128
BGLY301
BGLY302
BTHR305
BGLN360
BARG372
BPRO431
BPHE432
BSER433
BARG437
BASN438
BCYS439
BPHE440
BGLY441
BHOH510
BHOH511

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM C 500
ChainResidue
CARG101
CVAL117
CARG128
CGLY301
CGLY302
CTHR305
CTHR309
CARG372
CPRO431
CPHE432
CSER433
CARG437
CASN438
CCYS439
CPHE440
CGLY441
CALA445
CHOH503

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HEM D 500
ChainResidue
DARG101
DVAL117
DARG128
DGLY301
DGLY302
DTHR305
DTHR309
DARG372
DPRO431
DPHE432
DSER433
DARG437
DASN438
DCYS439
DPHE440
DGLY441

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
AGLN297
BGLN297
CGLN297
DGLN297

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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
AGLU304
ATHR305

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
BGLU304
BTHR305

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
CGLU304
CTHR305

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1akd
ChainResidueDetails
DGLU304
DTHR305

219140

PDB entries from 2024-05-01

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