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2BN4

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003958molecular_functionNADPH-hemoprotein reductase activity
A0003959molecular_functionNADPH dehydrogenase activity
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005741cellular_componentmitochondrial outer membrane
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006694biological_processsteroid biosynthetic process
A0006696biological_processergosterol biosynthetic process
A0008202biological_processsteroid metabolic 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
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006694biological_processsteroid biosynthetic process
B0006696biological_processergosterol biosynthetic process
B0008202biological_processsteroid metabolic 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 Residues25
DetailsBINDING SITE FOR RESIDUE FAD A 750
ChainResidue
AGLY364
ATHR457
ASER458
AILE459
AGLU461
AVAL474
AVAL475
AGLY476
AVAL477
ATHR478
ATHR479
APRO365
ATHR543
ATRP691
AFMN751
AHOH2018
AHOH2032
AHOH2033
ATYR405
APHE406
AASN407
AARG439
ATYR440
ATYR441
ASER442

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER67
AGLN68
ATHR69
ATHR71
AALA72
ASER116
ATHR117
ATYR118
AGLY119
ALEU152
AGLY153
AASN154
ATYR157
AGLU158
APHE159
APHE160
AASN161
AVAL690
AFAD750

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP A 753
ChainResidue
AARG285
AILE459
AGLU461
APRO541
ATHR543
ASER580
AARG581
ASER610
AARG611
ALYS617
ATYR619
AGLN621
AASP646
ALYS648
AGLY649
AMET650
ATRP691
AHOH2028

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE FAD B 750
ChainResidue
BHIS306
BGLY364
BTYR405
BPHE406
BARG439
BTYR440
BTYR441
BSER442
BTHR457
BSER458
BILE459
BGLU461
BPHE463
BVAL474
BVAL475
BGLY476
BVAL477
BTHR478
BTHR479
BTHR543
BTRP691
BFMN751
BNAP753
BHOH2015
BHOH2021
BHOH2022

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 751
ChainResidue
BASN154
BTYR157
BGLU158
BPHE159
BPHE160
BASN161
BVAL690
BFAD750
BSER67
BGLN68
BTHR69
BGLY70
BTHR71
BALA72
BSER116
BTHR117
BTYR118
BLEU152
BGLY153

site_idAC6
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAP B 753
ChainResidue
BARG285
BILE459
BGLU461
BPRO541
BTHR543
BSER580
BARG581
BSER610
BARG611
BLYS617
BTYR619
BGLN621
BASP646
BGLY649
BMET650
BTRP691
BFAD750
BHOH2022

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues286
DetailsDomain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues526
DetailsDomain: {"description":"FAD-binding FR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16407065","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19483672","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16407065","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues34
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16407065","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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

245663

PDB entries from 2025-12-03

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