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2BF4

A second FMN-binding site in yeast NADPH-cytochrome P450 reductase suggests a novel mechanism of electron transfer by diflavin reductases.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003958molecular_functionNADPH-hemoprotein reductase activity
A0003959molecular_functionNADPH dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006696biological_processergosterol biosynthetic process
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016126biological_processsterol biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
B0003958molecular_functionNADPH-hemoprotein reductase activity
B0003959molecular_functionNADPH dehydrogenase activity
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005741cellular_componentmitochondrial outer membrane
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006696biological_processergosterol biosynthetic process
B0009055molecular_functionelectron transfer activity
B0010181molecular_functionFMN binding
B0016126biological_processsterol biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 760
ChainResidue
ASER282
AASP284
AARG285
AASN582
AHOH2107

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 761
ChainResidue
AASP626
BPRO337
BLEU338

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 762
ChainResidue
BARG553

site_idAC4
Number of Residues30
DetailsBINDING SITE FOR RESIDUE FAD A 750
ChainResidue
AHIS306
AGLY364
APRO365
ATYR405
APHE406
AASN407
AARG439
ATYR440
ATYR441
ASER442
ATHR457
ASER458
AILE459
AGLU461
APHE463
AVAL474
AVAL475
AGLY476
AVAL477
ATHR478
ATHR479
ATRP691
AFMN751
AFMN752
AHOH2060
AHOH2096
AHOH2097
AHOH2098
AHOH2101
AHOH2106

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER67
AGLN68
ATHR69
AGLY70
ATHR71
AALA72
ASER116
ATHR117
ATYR118
AGLY119
AGLU120
ALEU152
AGLY153
AASN154
ATYR157
AGLU158
APHE159
APHE160
AASN161
AVAL690
AFAD750
AHOH2103

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FMN A 752
ChainResidue
ATHR69
AASP74
ATYR75
ALYS78
AASP187
AASP193
APRO365
AVAL366
ASER367
AFAD750
AHOH2033
AHOH2096
AHOH2100
AHOH2101
AHOH2103
AHOH2104

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE NAP A 753
ChainResidue
AARG285
AILE459
AGLU461
APRO541
AGLY542
ATHR543
ASER580
AARG581
ASER610
AARG611
ALYS617
ATYR619
AGLN621
AASP646
AGLY649
AMET650
AHOH2080
AHOH2105
AHOH2106

site_idAC8
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD B 750
ChainResidue
BTYR405
BPHE406
BASN407
BARG439
BTYR440
BTYR441
BSER442
BTHR457
BSER458
BILE459
BGLU461
BVAL474
BVAL475
BGLY476
BVAL477
BTHR478
BTHR479
BTRP691
BFMN751
BFMN752
BHOH2043
BHIS306
BGLY364
BPRO365

site_idAC9
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN B 751
ChainResidue
BSER67
BGLN68
BTHR69
BGLY70
BTHR71
BALA72
BSER116
BTHR117
BTYR118
BGLY119
BLEU152
BGLY153
BASN154
BTYR157
BPHE159
BPHE160
BASN161
BASP187
BVAL690
BFAD750

site_idBC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FMN B 752
ChainResidue
BTHR71
BASP74
BTYR75
BLYS78
BASP187
BASP193
BPRO365
BVAL366
BSER367
BPRO434
BFAD750
BHOH2008
BHOH2043

site_idBC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP B 753
ChainResidue
BARG285
BILE459
BGLU461
BPRO541
BGLY542
BTHR543
BSER580
BARG581
BSER610
BARG611
BLYS617
BTYR619
BGLN621
BASP646
BGLY649
BMET650
BTRP691
BHOH2020

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1332
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
APRO25-TRP691
BPRO25-TRP691

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16407065, ECO:0000269|PubMed:19483672
ChainResidueDetails
AGLN68
ATHR117
AGLY153
BGLN68
BTHR117
BGLY153

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16407065
ChainResidueDetails
APHE79
AALA647
BPHE79
BALA647

site_idSWS_FT_FI4
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:16407065
ChainResidueDetails
AGLY188
BGLY188
BASN286
BTYR440
BSER458
BVAL477
BGLY544
BARG611
BVAL618
BTRP691
AASN286
ATYR440
ASER458
AVAL477
AGLY544
AARG611
AVAL618
ATRP691

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ASER667
BSER667

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
ASER444

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ndh
ChainResidueDetails
BSER444

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PDB entries from 2024-11-06

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