Structure of PDB 2iya Chain A

Receptor sequence
>2iyaA (length=392) Species: 1890 (Streptomyces antibioticus) [Search protein sequence]
TPRHISFFNIPGHGHVNPSLGIVQELVARGHRVSYAITDEFAAQVKAAGA
TPVVYDSILPKESNPEESWPEDQESAMGLFLDEAVRVLPQLEDAYADDRP
DLIVYDIASWPAPVLGRKWDIPFVQLSPTFVAYEGFEEDVPAVQDPTAED
GLVRFFTRLSAFLEEHGVDTPATEFLIAPNRCIVALPRTFQIKGDTVGDN
YTFVGPTYGDRSHQGTWEGPGDGRPVLLIALGSAFTDHLDFYRTCLSAVD
GLDWHVVLSVGRFVDPADLGEVPPNVEVHQWVPQLDILTKASAFITHAGM
GSTMEALSNAVPMVAVPQIAEQTMNAERIVELGLGRHIPRDQVTAEKLRE
AVLAVASDPGVAERLAAVRQEIREAGGARAAADILEGILAEA
3D structure
PDB2iya The Crystal Structure of Two Macrolide Glycosyltransferases Provides a Blueprint for Host Cell Antibiotic Immunity.
ChainA
Resolution1.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.-
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 UDP A G24 S264 W312 V313 Q315 H328 G330 G332 S333 E336 G14 S233 W281 V282 Q284 H297 G299 G301 S302 E305
BS02 ZIO A H25 W79 Q83 A86 M87 F90 T139 F140 F146 L207 A351 E352 M355 H15 W69 Q73 A76 M77 F80 T129 F130 F136 L176 A320 E321 M324
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008194 UDP-glycosyltransferase activity
GO:0016740 transferase activity
GO:0016758 hexosyltransferase activity
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2iya, PDBe:2iya, PDBj:2iya
PDBsum2iya
PubMed17376874
UniProtQ3HTL7

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