Structure of PDB 1ylu Chain B

Receptor sequence

>1yluB (length=216) Species: 562 (Escherichia coli)

DIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVA
STEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQ
EDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFL
LGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNA
TLPKSRLPQNITLTEV

3D structure

• PDB: 1ylu Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K14 K74 E165
• Catalytic site (residue number reindexed from 1): K13 K73 E164
• 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	B	S39 S40 N42	S38 S39 N41
BS02	ACT	B	T41 F124	T40 F123
BS03	FMN	B	R10 H11 S12 K14 N71 P163 I164 E165 G166 K205 R207	R9 H10 S11 K13 N70 P162 I163 E164 G165 K204 R206

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:1ylu, PDBe:1ylu, PDBj:1ylu
• PDBsum: 1ylu
• PubMed: 15684426
• UniProt: P38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)