Structure of PDB 1iin Chain D

Receptor sequence
>1iinD (length=289) Species: 28901 (Salmonella enterica) [Search protein sequence]
MKTRKGIILAGGSGTRLYPVTMAVSQQLLPIYDKPMIYYPLSTLMLAGIR
DILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFI
GHDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVE
FDQKGTAVSLEEKPLQPKSNYAVTGLYFYDNSVVEMAKNLKPSARGELEI
TDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLK
VSCPEEIAFRKNFINAQQVIELAGPLSKNDYGKYLLKMV
3D structure
PDB1iin Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization.
ChainD
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.24: glucose-1-phosphate thymidylyltransferase.
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 UPG D L9 G11 Q83 P86 G88 D111 Y146 G147 E162 K163 V173 R195 L9 G11 Q83 P86 G88 D111 Y146 G147 E162 K163 V173 R195
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008879 glucose-1-phosphate thymidylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009058 biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009243 O antigen biosynthetic process
GO:0019305 dTDP-rhamnose biosynthetic process
GO:0045226 extracellular polysaccharide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1iin, PDBe:1iin, PDBj:1iin
PDBsum1iin
PubMed11373625
UniProtP26393|RMLA_SALTY Glucose-1-phosphate thymidylyltransferase (Gene Name=rmlA)

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