Structure of PDB 6yca Chain C

Receptor sequence
>6ycaC (length=388) Species: 36809 (Mycobacteroides abscessus) [Search protein sequence]
VTDIRFLQSRAEHERAFTVFWRAMVGLPAADELLELGRYLGAFVQGELIG
GADSYTSWLTVPGGSRVPHAAVTHIGVLPTHTRRGILTALVTRQLTDIAG
RGEIVASLRASEAVIYRRFGYGIATSSATYRIQRRRAAPLRPIDTGAIAL
LDAAASPEGLAAIYERAAWTGSVARPPQWWRLHELFDAADPVKPYVVTHP
DGYVRYRPQDTAEWFSSSARTISVDDLVAHSDEAYRALVGHLLDLDLVDV
IELGPRPIDDPLPHLVTDPRAVAVAGIRDETWLRLVDVEAALAARTYTDG
APVVIEVQDTLLPHNAARFSVSSDKVRRTQHTPDISVDVAALGSVYLGGN
TWTRLERAGLVSAQSPGAIRAADALFSTGTQPFAGTNF
3D structure
PDB6yca Structural analysis of the N-acetyltransferase Eis1 from Mycobacterium abscessus reveals the molecular determinants of its incapacity to modify aminoglycosides.
ChainC
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.-
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 ACO C A45 M46 I102 G103 V104 T109 R110 G112 I113 L114 T115 L135 R136 S138 E139 V141 Y143 R145 A23 M24 I75 G76 V77 T82 R83 G85 I86 L87 T88 L108 R109 S111 E112 V114 Y116 R118
BS02 ACO C D273 L274 D246 L247
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:6yca, PDBe:6yca, PDBj:6yca
PDBsum6yca
PubMed32860271
UniProtA0A418LDP6

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