Structure of PDB 3x22 Chain A

Receptor sequence

>3x22A (length=217) Species: 83333 (Escherichia coli K-12)

MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIV
ASTEEGKARVAKSAAGNYVFSERKMLDASHVVVFCAKTAMDDVWLKLVVD
QEDADGRFATPEAKAANDKGRKAWADMHRKDLHDDAEWMAKQVYLNVGNF
LLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFN
ATLPKSRLPQNITLTEV

3D structure

• PDB: 3x22 Structural basis of Escherichia coli nitroreductase NfsB triple mutants engineered for improved activity and regioselectivity toward the prodrug CB1954
• Chain: A
• Resolution: 2.001 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K14 K74 E165
• Catalytic site (residue number reindexed from 1): K14 K74 E165
• 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 P163 I164 E165 G166 K205 R207	R10 H11 S12 K14 P163 I164 E165 G166 K205 R207
BS02	FMN	A	S39 S40 N42 W124	S39 S40 N42 W124

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:3x22, PDBe:3x22, PDBj:3x22
• PDBsum: 3x22
• UniProt: P38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)