Structure of PDB 2y6r Chain D

Receptor sequence
>2y6rD (length=365) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
SDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHK
GSGQEAMKKAGLLQTYYDLALPMGVNIADAAGNILSTKNVKPENRFDNPE
INRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLV
ILANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEINCPGFFQLCNGNRL
MASHQGNLLFANPNNNGALHFGISFKTPDEWQVDFQNRNSVVDFLLKEFS
DWDERYKELIHTTLSFVGLATRIFPLEKPWKSKRPLPITMIGDAAHLMPP
FAGQGVNSGLVDALILSDNLADGKFNSIEEAVKNYEQQMFIYGKEAQEES
TQNEIEMFKPDFTFQ
3D structure
PDB2y6r Structural Basis for a New Tetracycline Resistance Mechanism Relying on the Tetx Monooxygenase.
ChainD
Resolution3.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.231: tetracycline 11a-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 FAD D I22 G25 V27 Y45 E46 R47 L60 R117 R137 K138 L139 N168 G169 Q192 G310 D311 P318 G321 Q322 G323 V324 I8 G11 V13 Y31 E32 R33 L46 R103 R123 K124 L125 N154 G155 Q178 G292 D293 P300 G303 Q304 G305 V306
BS02 CTC D R213 F224 P318 R199 F210 P300
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004497 monooxygenase activity
GO:0071949 FAD binding
Biological Process
GO:0046677 response to antibiotic
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2y6r, PDBe:2y6r, PDBj:2y6r
PDBsum2y6r
PubMed21402075
UniProtQ93L51|TETX_BACT4 Flavin-dependent monooxygenase (Gene Name=tetX2)

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