Structure of PDB 7x32 Chain E

Receptor sequence

>7x32E (length=217) Species: 562 (Escherichia coli)

MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIV
ASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVD
QEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNF
LLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFN
ATLPKSRLPQNITLTEV

3D structure

• PDB: 7x32 Structural basis for the transformation of the traditional medicine berberine by bacterial nitroreductase.
• Chain: E
• Resolution: 1.829 Å

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	E	R10 H11 S12 K14 N71 K74 P163 I164 E165 G166 K205 R207	R10 H11 S12 K14 N71 K74 P163 I164 E165 G166 K205 R207
BS02	BER	E	T41 N42 E102 R107 N117 R121 F124	T41 N42 E102 R107 N117 R121 F124
BS03	FMN	E	P38 S39 S40 N42	P38 S39 S40 N42
BS04	BER	E	K14 F70	K14 F70

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

External links

• PDB: RCSB:7x32, PDBe:7x32, PDBj:7x32
• PDBsum: 7x32
• PubMed: 36189746
• UniProt: P38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)