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3QE2

Crystal Structure of Human NADPH-Cytochrome P450 Reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003958molecular_functionNADPH-hemoprotein reductase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006805biological_processxenobiotic metabolic process
A0009725biological_processresponse to hormone
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0022900biological_processelectron transport chain
A0032770biological_processpositive regulation of monooxygenase activity
A0043231cellular_componentintracellular membrane-bounded organelle
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0090346biological_processcellular organofluorine metabolic process
B0003958molecular_functionNADPH-hemoprotein reductase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006805biological_processxenobiotic metabolic process
B0009725biological_processresponse to hormone
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0022900biological_processelectron transport chain
B0032770biological_processpositive regulation of monooxygenase activity
B0043231cellular_componentintracellular membrane-bounded organelle
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0090346biological_processcellular organofluorine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues32
DetailsBINDING SITE FOR RESIDUE FAD A 752
ChainResidue
AHOH1
ATYR458
ATYR459
ASER460
ACYS475
AALA476
AVAL477
AVAL479
ATYR481
AGLY491
AVAL492
AHOH6
AALA493
ATHR494
ATRP679
AFMN751
AHOH875
AHOH901
AHOH914
AHOH932
AHOH938
AHOH1006
AHOH34
AHOH1050
AHOH1078
BASN506
AHOH56
AHOH57
AHOH60
AHIS322
AARG427
AARG457

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER89
AGLN90
ATHR91
AGLY92
ATHR93
AALA94
AALA141
ATHR142
ATYR143
AGLY144
AGLY146
ALEU176
AGLY177
AASN178
ATYR181
AHIS183
APHE184
AASN185
ALEU215
AHOH737
AFAD752
AHOH777
AHOH796
AHOH871

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP A 753
ChainResidue
AHOH12
AHOH33
AARG301
AGLY537
ATHR538
ACYS569
AARG570
ASER599
AARG600
ALYS605
ATYR607
AGLN609
AASN637
AMET638
AASP641
AHOH681
AHOH828
AHOH837
AHOH862
AHOH917
AHOH1070
AHOH1143

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 762
ChainResidue
AASP255
AASN595
AHOH735
AHOH876
AHOH877
AHOH910
AHOH912

site_idAC5
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD B 752
ChainResidue
BTHR494
BALA541
BTRP679
BHOH692
BHOH695
BHOH698
BHOH704
BFMN751
BHOH955
BHOH974
BHOH1016
BHIS322
BARG427
BARG457
BTYR458
BTYR459
BSER460
BCYS475
BALA476
BVAL477
BVAL479
BTYR481
BGLY491
BVAL492
BALA493

site_idAC6
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FMN B 751
ChainResidue
BSER89
BGLN90
BTHR91
BGLY92
BTHR93
BALA94
BALA141
BTHR142
BTYR143
BGLY144
BGLY146
BLEU176
BGLY177
BASN178
BTYR181
BHIS183
BPHE184
BASN185
BASP211
BLEU215
BFAD752
BHOH758
BHOH856
BHOH982
BHOH1021

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAP B 753
ChainResidue
BARG301
BGLY537
BTHR538
BCYS569
BARG570
BSER599
BARG600
BLYS605
BTYR607
BGLN609
BMET638
BASP641
BHOH686
BHOH705
BHOH763
BHOH1003

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:10048323, ECO:0000269|PubMed:21808038
ChainResidueDetails
ASER89
AALA141
ALEU176
AASP211
BSER89
BALA141
BLEU176
BASP211

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:21808038
ChainResidueDetails
AARG301
BASP641
ATHR538
ASER599
ALYS605
AASP641
BARG301
BTHR538
BSER599
BLYS605

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:19483672, ECO:0000269|PubMed:21808038
ChainResidueDetails
AARG427
BTYR481
BGLY491
BTRP679
AARG457
ACYS475
ATYR481
AGLY491
ATRP679
BARG427
BARG457
BCYS475

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PDB entries from 2024-07-10

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