Structure of PDB 1oo5 Chain A

Receptor sequence

>1oo5A (length=217) Species: 562 (Escherichia coli)

MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIV
ASTEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVD
QEDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNF
LLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFN
ATLPKSRLPQNITLTEV

3D structure

• PDB: 1oo5 Studies on the Nitroreductase Prodrug-Activating System. Crystal Structures of Complexes with the Inhibitor Dicoumarol and Dinitrobenzamide Prodrugs and of the Enzyme Active Form
• Chain: A
• Resolution: 2.5 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 N71 K74 V162 P163 I164 E165 G166 K205 R207	R10 H11 S12 N71 K74 V162 P163 I164 E165 G166 K205 R207
BS02	FMN	A	S39 S40 N42 Q142	S39 S40 N42 Q142

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:1oo5, PDBe:1oo5, PDBj:1oo5
• PDBsum: 1oo5
• PubMed: 12954054
• UniProt: P38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)