Structure of PDB 2y6r Chain A

Receptor sequence

>2y6rA (length=366) Species: 818 (Bacteroides thetaiotaomicron)

SDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDLHK
GSGQEAMKKAGLLQTYYDLALPMGVNIADAAGNILSTKNVKPENRFDNPE
INRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLV
ILANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEINCPGFFQLCNGNRL
MASHQGNLLFANPNNNGALHFGISFKTPDEWTQVDFQNRNSVVDFLLKEF
SDWDERYKELIHTTLSFVGLATRIFPLEKPWKSKRPLPITMIGDAAHLMP
PFAGQGVNSGLVDALILSDNLADGKFNSIEEAVKNYEQQMFIYGKEAQEE
STQNEIEMFKPDFTFQ

3D structure

• PDB: 2y6r Structural Basis for a New Tetracycline Resistance Mechanism Relying on the Tetx Monooxygenase.
• Chain: A
• Resolution: 3.1 Å

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	A	I22 G23 G25 P26 V27 Y45 E46 R47 R117 L139 N168 G169 Q192 G310 D311 P318 G321 Q322 G323 V324	I8 G9 G11 P12 V13 Y31 E32 R33 R103 L125 N154 G155 Q178 G293 D294 P301 G304 Q305 G306 V307
BS02	CTC	A	Q192 R213 F224 P318 F319 A320 G321 M375	Q178 R199 F210 P301 F302 A303 G304 M358

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

External links

• PDB: RCSB:2y6r, PDBe:2y6r, PDBj:2y6r
• PDBsum: 2y6r
• PubMed: 21402075
• UniProt: Q93L51|TETX_BACT4 Flavin-dependent monooxygenase (Gene Name=tetX2)