Structure of PDB 6teg Chain AAA

Receptor sequence
>6tegAAA (length=338) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MMKIGVFVPIGNNGWLISTHAPQYMPTFELNKAIVQKAEHYHFDFALSMI
KLRGFGGKTEFWDHNLESFTLMAGLAAVTSRIQIYATAATLTLPPAIVAR
MAATIDSISGGRFGVNLVTGWQKPEYEQMGIWPGDDYFSRRYDYLTEYVQ
VLRDLWGTGKSDFKGDFFTMNDCRVSPQPSVPMKVICAGQSDAGMAFSAR
YADFNFCFGKGVNTPTAFAPTAARMKQAAEQTGRDVGSYVLFMVIADETD
DAARAKWEHYKAGADEEALSWLTDPTSAVNINMGTLVGSYASVARMLDEV
ASVPGAEGVLLTFDDFLSGIETFGERIQPLMQCRAHLP
3D structure
PDB6teg Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases.
ChainAAA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.99.46: pyrimidine monooxygenase.
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 AAA M67 I68 V136 R159 Y160 A206 Q208 S209 M49 I50 V118 R141 Y142 A188 Q190 S191
BS02 URA AAA F25 W33 M67 K69 F7 W15 M49 K51
BS03 OXY AAA L65 M67 T105 N134 L47 M49 T87 N116
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0008726 alkanesulfonate monooxygenase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0052614 uracil oxygenase activity
Biological Process
GO:0006208 pyrimidine nucleobase catabolic process
GO:0006210 thymine catabolic process
GO:0006212 uracil catabolic process
GO:0019740 nitrogen utilization
GO:0046306 alkanesulfonate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6teg, PDBe:6teg, PDBj:6teg
PDBsum6teg
PubMed32066967
UniProtP75898|RUTA_ECOLI Pyrimidine monooxygenase RutA (Gene Name=rutA)

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