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8V5B

Structure of the oxygen-insensitive NAD(P)H-dependent nitroreductase NfsB_Ec F70A/F108Y in complex with FMN

Functional Information from GO Data
ChainGOidnamespacecontents
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0004155molecular_function6,7-dihydropteridine reductase activity
A0005829cellular_componentcytosol
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046256biological_process2,4,6-trinitrotoluene catabolic process
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0004155molecular_function6,7-dihydropteridine reductase activity
B0005829cellular_componentcytosol
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046256biological_process2,4,6-trinitrotoluene catabolic process
C0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
C0004155molecular_function6,7-dihydropteridine reductase activity
C0005829cellular_componentcytosol
C0010181molecular_functionFMN binding
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0046256biological_process2,4,6-trinitrotoluene catabolic process
D0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
D0004155molecular_function6,7-dihydropteridine reductase activity
D0005829cellular_componentcytosol
D0010181molecular_functionFMN binding
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0046256biological_process2,4,6-trinitrotoluene catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11020276","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11491290","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15684426","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q01234","evidenceCode":"ECO:0000250"}]}
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

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PDB entries from 2025-10-29

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