Structure of PDB 1ylu Chain A

Receptor sequence
>1yluA (length=216) Species: 562 (Escherichia coli) [Search protein sequence]
DIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVA
STEEGKARVAKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQ
EDADGRFATPEAKAANDKGRKFFADMHRKDLHDDAEWMAKQVYLNVGNFL
LGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFNA
TLPKSRLPQNITLTEV
3D structure
PDB1ylu Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme.
ChainA
Resolution2.0 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 ACT A T41 F124 T40 F123
BS02 ACT A E54 K57 L76 E53 K56 L75
BS03 FMN A R10 H11 S12 K14 N71 K74 P163 I164 E165 G166 K205 R9 H10 S11 K13 N70 K73 P162 I163 E164 G165 K204
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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Biological Process

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Cellular Component
External links
PDB RCSB:1ylu, PDBe:1ylu, PDBj:1ylu
PDBsum1ylu
PubMed15684426
UniProtP38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)

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