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7XWW

Crystal structure of NTR in complex with BN-XB

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
H0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
H0004155molecular_function6,7-dihydropteridine reductase activity
H0005829cellular_componentcytosol
H0010181molecular_functionFMN binding
H0016020cellular_componentmembrane
H0016491molecular_functionoxidoreductase activity
H0042802molecular_functionidentical protein binding
H0042803molecular_functionprotein homodimerization activity
H0046256biological_process2,4,6-trinitrotoluene catabolic process
I0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
I0004155molecular_function6,7-dihydropteridine reductase activity
I0005829cellular_componentcytosol
I0010181molecular_functionFMN binding
I0016020cellular_componentmembrane
I0016491molecular_functionoxidoreductase activity
I0042802molecular_functionidentical protein binding
I0042803molecular_functionprotein homodimerization activity
I0046256biological_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

site_idMCSA4
Number of Residues3
DetailsM-CSA 211
ChainResidueDetails

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PDB entries from 2025-11-05

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