Structure of PDB 2y6q Chain B

Receptor sequence
>2y6qB (length=368) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
LLSDKNVAIIGGGPVGLTMAKLLQQNGIDVSVYERDNDREARIFGGTLDL
HKGSGQEAMKKAGLLQTYYDLALPMGVNIADEKGNILSTKNVKPENRFDN
PEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETAD
LVILANGGMSKVRKFVTDTEVEETGTFNIQADIHQPEINCPGFFQLCNGN
RLMASHQGNLLFANPNNNGALHFGISFKTPDEWTQVDFQNRNSVVDFLLK
EFSDWDERYKELIHTTLSFVGLATRIFPLEKPWKSKRPLPITMIGDAAHL
MPPFAGQGVNSGLVDALILSDNLADGKFNSIEEAVKNYEQQMFIYGKEAQ
EESTQNEIEMFKPDFTFQ
3D structure
PDB2y6q Structural Basis for a New Tetracycline Resistance Mechanism Relying on the Tetx Monooxygenase.
ChainB
Resolution2.37 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 B G25 P26 V27 E46 R47 R117 R137 L139 N168 G169 D311 P318 G321 Q322 V324 G13 P14 V15 E34 R35 R105 R125 L127 N156 G157 D296 P303 G306 Q307 V309
BS02 I7T B F224 G236 P318 F319 A320 G321 F212 G224 P303 F304 A305 G306
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:2y6q, PDBe:2y6q, PDBj:2y6q
PDBsum2y6q
PubMed21402075
UniProtQ93L51|TETX_BACT4 Flavin-dependent monooxygenase (Gene Name=tetX2)

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