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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7X32

Crystal structure of E. coli NfsB in complex with berberine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0004155molecular_function6,7-dihydropteridine reductase activity
A0005829cellular_componentcytosol
A0008753molecular_functionNADPH dehydrogenase (quinone) activity
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0004155molecular_function6,7-dihydropteridine reductase activity
B0005829cellular_componentcytosol
B0008753molecular_functionNADPH dehydrogenase (quinone) activity
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
C0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
C0004155molecular_function6,7-dihydropteridine reductase activity
C0005829cellular_componentcytosol
C0008753molecular_functionNADPH dehydrogenase (quinone) activity
C0010181molecular_functionFMN binding
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
D0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
D0004155molecular_function6,7-dihydropteridine reductase activity
D0005829cellular_componentcytosol
D0008753molecular_functionNADPH dehydrogenase (quinone) activity
D0010181molecular_functionFMN binding
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
E0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
E0004155molecular_function6,7-dihydropteridine reductase activity
E0005829cellular_componentcytosol
E0008753molecular_functionNADPH dehydrogenase (quinone) activity
E0010181molecular_functionFMN binding
E0016020cellular_componentmembrane
E0016491molecular_functionoxidoreductase activity
E0042802molecular_functionidentical protein binding
E0042803molecular_functionprotein homodimerization activity
E0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
F0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
F0004155molecular_function6,7-dihydropteridine reductase activity
F0005829cellular_componentcytosol
F0008753molecular_functionNADPH dehydrogenase (quinone) activity
F0010181molecular_functionFMN binding
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0042802molecular_functionidentical protein binding
F0042803molecular_functionprotein homodimerization activity
F0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
G0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
G0004155molecular_function6,7-dihydropteridine reductase activity
G0005829cellular_componentcytosol
G0008753molecular_functionNADPH dehydrogenase (quinone) activity
G0010181molecular_functionFMN binding
G0016020cellular_componentmembrane
G0016491molecular_functionoxidoreductase activity
G0042802molecular_functionidentical protein binding
G0042803molecular_functionprotein homodimerization activity
G0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
H0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
H0004155molecular_function6,7-dihydropteridine reductase activity
H0005829cellular_componentcytosol
H0008753molecular_functionNADPH dehydrogenase (quinone) activity
H0010181molecular_functionFMN binding
H0016020cellular_componentmembrane
H0016491molecular_functionoxidoreductase activity
H0042802molecular_functionidentical protein binding
H0042803molecular_functionprotein homodimerization activity
H0050136molecular_functionNADH dehydrogenase (quinone) (non-electrogenic) activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11020276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11491290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12954054","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684426","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25917861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36189746","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"1760","lastPage":"1766","volume":"50","journal":"Process Biochem.","title":"Structural basis of Escherichia coli nitroreductase NfsB triple mutants engineered for improved activity and regioselectivity toward the prodrug CB1954.","authors":["Bai J.","Yang J.","Zhou Y.","Yang Q."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.procbio.2015.08.012"}]}},{"source":"PDB","id":"1DS7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OO5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OO6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OOQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YLU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X21","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X22","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X32","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q01234","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11491290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12954054","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684426","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25917861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36189746","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"1760","lastPage":"1766","volume":"50","journal":"Process Biochem.","title":"Structural basis of Escherichia coli nitroreductase NfsB triple mutants engineered for improved activity and regioselectivity toward the prodrug CB1954.","authors":["Bai J.","Yang J.","Zhou Y.","Yang Q."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.procbio.2015.08.012"}]}},{"source":"PDB","id":"1ICR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OO5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OO6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OOQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YLU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X21","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X22","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X32","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11020276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11491290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12954054","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684426","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25917861","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36189746","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2015","firstPage":"1760","lastPage":"1766","volume":"50","journal":"Process Biochem.","title":"Structural basis of Escherichia coli nitroreductase NfsB triple mutants engineered for improved activity and regioselectivity toward the prodrug CB1954.","authors":["Bai J.","Yang J.","Zhou Y.","Yang Q."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/j.procbio.2015.08.012"}]}},{"source":"PDB","id":"1DS7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ICV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IDT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OO5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OO6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OON","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OOQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YLR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X21","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3X22","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7X32","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
ALYS14electrostatic stabiliser, hydrogen bond donor
ALYS74electrostatic stabiliser, hydrogen bond donor
AGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA2
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
BLYS14electrostatic stabiliser, hydrogen bond donor
BLYS74electrostatic stabiliser, hydrogen bond donor
BGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA3
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
CLYS14electrostatic stabiliser, hydrogen bond donor
CLYS74electrostatic stabiliser, hydrogen bond donor
CGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA4
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
DLYS14electrostatic stabiliser, hydrogen bond donor
DLYS74electrostatic stabiliser, hydrogen bond donor
DGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA5
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
ELYS14electrostatic stabiliser, hydrogen bond donor
ELYS74electrostatic stabiliser, hydrogen bond donor
EGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA6
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
FLYS14electrostatic stabiliser, hydrogen bond donor
FLYS74electrostatic stabiliser, hydrogen bond donor
FGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA7
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
GLYS14electrostatic stabiliser, hydrogen bond donor
GLYS74electrostatic stabiliser, hydrogen bond donor
GGLU165electrostatic stabiliser, hydrogen bond donor
site_idMCSA8
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails
HLYS14electrostatic stabiliser, hydrogen bond donor
HLYS74electrostatic stabiliser, hydrogen bond donor
HGLU165electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2026-09-23

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