Structure of PDB 7x32 Chain A

Receptor sequence
>7x32A (length=216) Species: 562 (Escherichia coli) [Search protein sequence]
DIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVA
STEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQ
EDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFL
LGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNA
TLPKSRLPQNITLTEV
3D structure
PDB7x32 Structural basis for the transformation of the traditional medicine berberine by bacterial nitroreductase.
ChainA
Resolution1.829 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 1.-.-.-
1.5.1.34: 6,7-dihydropteridine reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FMN A R10 H11 S12 K14 N71 P163 I164 E165 G166 K205 R207 R9 H10 S11 K13 N70 P162 I163 E164 G165 K204 R206
BS02 FMN A P38 S39 S40 N42 P37 S38 S39 N41
BS03 BER A K14 F70 K13 F69
Gene Ontology
Molecular Function
GO:0003955 NAD(P)H dehydrogenase (quinone) activity
GO:0004155 6,7-dihydropteridine reductase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0046857 oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
Biological Process
GO:0046256 2,4,6-trinitrotoluene catabolic process
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:7x32, PDBe:7x32, PDBj:7x32
PDBsum7x32
PubMed36189746
UniProtP38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)

[Back to BioLiP]