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3QFC

Crystal Structure of Human NADPH-Cytochrome P450 (V492E mutant)

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
ATYR459
ASER460
ACYS475
AALA476
AVAL477
AVAL479
ATYR481
AGLY491
AGLU492
AALA493
AHOH3
ATHR494
ATRP679
AHOH721
AHOH735
AFMN751
AHOH835
AHOH866
AHOH955
AHOH988
AHOH1059
AHOH6
AHOH1086
AHOH1107
AHOH1189
AHOH33
AHOH55
AHIS322
AARG427
AARG457
ATYR458

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
AHOH31
ASER89
AGLN90
ATHR91
AGLY92
ATHR93
AALA94
AALA141
ATHR142
ATYR143
AGLY144
AGLY146
ALEU176
AGLY177
AASN178
ATYR181
AHIS183
APHE184
AASN185
ALEU215
AHOH713
AFAD752
AHOH807
AHOH933

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAP A 753
ChainResidue
AHOH19
AARG301
AGLY537
ATHR538
ACYS569
AARG570
ASER599
AARG600
ALYS605
ATYR607
AGLN609
AASN637
AMET638
AASP641
AHOH683
AHOH776
AHOH980
AHOH1109
AHOH1124

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 762
ChainResidue
AHOH34
AASN595
AHOH710
AHOH912
AHOH990
AHOH1190
AHOH1191

site_idAC5
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FAD B 752
ChainResidue
BHOH711
BFMN751
BHOH760
BHOH776
BHIS322
BARG427
BARG457
BTYR458
BTYR459
BSER460
BCYS475
BALA476
BVAL477
BVAL479
BGLY491
BGLU492
BALA493
BTHR494
BALA541
BTRP679
BHOH702

site_idAC6
Number of Residues22
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
BHOH705
BFAD752

site_idAC7
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP B 753
ChainResidue
BARG301
BGLY537
BTHR538
BCYS569
BARG570
BSER599
BARG600
BLYS605
BTYR607
BGLN609
BARG636
BASN637
BMET638
BASP641
BTRP679
BSER680
BHOH706
BHOH721
BHOH782
BHOH800
BHOH831

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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