Structure of PDB 1icv Chain A

Receptor sequence
>1icvA (length=216) Species: 562 (Escherichia coli) [Search protein sequence]
DIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVA
STEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQ
EDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFL
LGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNA
TLPKSRLPQNITLTEV
3D structure
PDB1icv The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A R10 H11 S12 K14 N71 K74 P163 I164 E165 G166 K205 R207 R9 H10 S11 K13 N70 K73 P162 I163 E164 G165 K204 R206
BS02 NIO A S40 T41 F124 S39 T40 F123
BS03 NIO A F70 G166 F69 G165
BS04 FMN A P38 S39 S40 N42 P37 S38 S39 N41
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

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External links
PDB RCSB:1icv, PDBe:1icv, PDBj:1icv
PDBsum1icv
PubMed11491290
UniProtP38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)

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