Structure of PDB 3x21 Chain H

Receptor sequence
>3x21H (length=217) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSLNSQPWHFIV
ASTEEGKARVAKSAAGNYVFSERKMLDASHVVVFCAKTAMDDVWLKLVVD
QEDADGRFATPEAKAANDKGRKFWADMHRKDLHDDAEWMAKQVYLNVGNF
LLGVAALGLDAVPIEGFDAAILDAEFGLKEKGYTSLVVVPVGHHSVEDFN
ATLPKSRLPQNITLTEV
3D structure
PDB3x21 Altering the regioselectivity of a nitroreductase in the synthesis of arylhydroxylamines by structure-based engineering.
ChainH
Resolution3.002 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) 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 H S39 S40 N42 Q142 S39 S40 N42 Q142
BS02 FMN H H11 S12 K14 P163 I164 E165 G166 R207 H11 S12 K14 P163 I164 E165 G166 R207
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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Cellular Component
External links
PDB RCSB:3x21, PDBe:3x21, PDBj:3x21
PDBsum3x21
PubMed25917861
UniProtP38489|NFSB_ECOLI Oxygen-insensitive NAD(P)H nitroreductase (Gene Name=nfsB)

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