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6CSD

V308E mutant of cytochrome P450 2D6 complexed with prinomastat

Functional Information from GO Data
ChainGOidnamespacecontents
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008210biological_processestrogen metabolic process
A0009804biological_processcoumarin metabolic process
A0009820biological_processalkaloid metabolic process
A0009822biological_processalkaloid catabolic process
A0016020cellular_componentmembrane
A0016098biological_processmonoterpenoid metabolic process
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
A0019369biological_processarachidonate metabolic process
A0020037molecular_functionheme binding
A0033076biological_processisoquinoline alkaloid metabolic process
A0042178biological_processxenobiotic catabolic process
A0042572biological_processretinol metabolic process
A0042759biological_processlong-chain fatty acid biosynthetic process
A0046872molecular_functionmetal ion binding
A0062187molecular_functionanandamide 8,9 epoxidase activity
A0062188molecular_functionanandamide 11,12 epoxidase activity
A0062189molecular_functionanandamide 14,15 epoxidase activity
A0070989biological_processoxidative demethylation
A0090350biological_processnegative regulation of organofluorine metabolic process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006805biological_processxenobiotic metabolic process
B0008202biological_processsteroid metabolic process
B0008203biological_processcholesterol metabolic process
B0008210biological_processestrogen metabolic process
B0009804biological_processcoumarin metabolic process
B0009820biological_processalkaloid metabolic process
B0009822biological_processalkaloid catabolic process
B0016020cellular_componentmembrane
B0016098biological_processmonoterpenoid metabolic process
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
B0019369biological_processarachidonate metabolic process
B0020037molecular_functionheme binding
B0033076biological_processisoquinoline alkaloid metabolic process
B0042178biological_processxenobiotic catabolic process
B0042572biological_processretinol metabolic process
B0042759biological_processlong-chain fatty acid biosynthetic process
B0046872molecular_functionmetal ion binding
B0062187molecular_functionanandamide 8,9 epoxidase activity
B0062188molecular_functionanandamide 11,12 epoxidase activity
B0062189molecular_functionanandamide 14,15 epoxidase activity
B0070989biological_processoxidative demethylation
B0090350biological_processnegative regulation of organofluorine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue HEM A 601
ChainResidue
AARG101
AVAL374
AHIS376
ALEU399
APRO435
APHE436
ASER437
AARG441
ACYS443
ALEU444
AGLY445
AVAL119
ALEU448
APN0602
AHOH752
APHE120
ATRP128
AARG132
AALA305
ATHR309
ATHR313
AGLN364

site_idAC2
Number of Residues14
Detailsbinding site for residue PN0 A 602
ChainResidue
APHE120
ALEU121
AGLY212
AGLU216
AGLN244
AALA300
AASP301
ASER304
AALA305
AGLU308
ATHR309
APHE483
AHEM601
AHOH707

site_idAC3
Number of Residues9
Detailsbinding site for residue CPS A 603
ChainResidue
ALEU73
ATHR76
AGLU222
ALEU372
AGLY373
ATHR375
AILE396
APHE483
AHOH840

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 604
ChainResidue
AHIS258
AASP270
AGLU273
AGLU287

site_idAC5
Number of Residues2
Detailsbinding site for residue ZN A 605
ChainResidue
AHIS463
AHOH897

site_idAC6
Number of Residues2
Detailsbinding site for residue ZN A 606
ChainResidue
AASP422
AHIS426

site_idAC7
Number of Residues22
Detailsbinding site for residue HEM B 601
ChainResidue
BARG101
BVAL119
BPHE120
BTRP128
BARG132
BASP301
BALA305
BGLY306
BTHR309
BTHR313
BILE369
BVAL374
BHIS376
BPHE436
BSER437
BARG441
BCYS443
BLEU444
BGLY445
BLEU448
BPN0602
BHOH754

site_idAC8
Number of Residues14
Detailsbinding site for residue PN0 B 602
ChainResidue
BPHE120
BGLY212
BLEU213
BGLU216
BGLN244
BALA300
BASP301
BSER304
BALA305
BGLU308
BTHR309
BPHE483
BHEM601
BHOH705

site_idAC9
Number of Residues8
Detailsbinding site for residue CPS B 603
ChainResidue
BTHR76
BGLU222
BGLY373
BTHR375
BILE396
BPHE483
BHOH721
BHOH747

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 604
ChainResidue
BGLU273
BGLU287
BHIS258
BASP270

site_idAD2
Number of Residues2
Detailsbinding site for residue ZN B 605
ChainResidue
BGLU155
BCYS159

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN B 606
ChainResidue
BCYS191
BLEU255
BHIS258
BTHR272

Functional Information from PROSITE/UniProt
site_idPS00086
Number of Residues10
DetailsCYTOCHROME_P450 Cytochrome P450 cysteine heme-iron ligand signature. FSaGRRACLG
ChainResidueDetails
APHE436-GLY445

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP301
BASP301

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
ACYS443
BCYS443

237735

PDB entries from 2025-06-18

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