Structure of PDB 3sxn Chain F

Receptor sequence
>3sxnF (length=402) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
MITPRTLHTITDDDWTRIALLARFAFGDIEPEQTQAAWRSMVPEDATVVV
PDETDDAFVGQSLYLDMQLTVPGGEVLPVAGISFVAVAPTHRRRGVLRAM
YTELHDRIARAGYPLAVLTASEGGIYGRFGYGVATIEQHVSVDRRLAQFH
PAAPDPGGVRMLVPADHRDGLADIYDRWRRRTPGGLVRPDALWDDLLADR
PESRRGGGELFAFGHQDGYALYRVDRGPDGRRSAHVVELTAVTADAHAAL
WRALLGLDLIDRVSIGTHPHDPLPYLLTDPRQAQVTASADDLWIRIMNVP
AALEARRYQADLDVVLDVADGFRSDGGRFALQISGGRARCTTTDAPADIE
IDLDVLGGLYLGAHRVDGFAAANRLRSKDSELLQQFGAAFAGDMPAELGY
GF
3D structure
PDB3sxn Mycobacterium tuberculosis Eis protein initiates suppression of host immune responses by acetylation of DUSP16/MKP-7
ChainF
Resolution2.03 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L21
Catalytic site (residue number reindexed from 1) L21
Enzyme Commision number ?
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 COA F F26 V85 A86 V87 R92 R93 G95 L97 R98 S121 I125 Y126 R128 F26 V85 A86 V87 R92 R93 G95 L97 R98 S121 I125 Y126 R128
Gene Ontology
Molecular Function
GO:0008080 N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
GO:0034069 aminoglycoside N-acetyltransferase activity
Biological Process
GO:0030649 aminoglycoside antibiotic catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0044161 host cell cytoplasmic vesicle

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3sxn, PDBe:3sxn, PDBj:3sxn
PDBsum3sxn
PubMed22547814
UniProtA0QY29

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