Structure of PDB 1mp5 Chain D

Receptor sequence
>1mp5D (length=289) Species: 28901 (Salmonella enterica) [Search protein sequence]
MKTRKGIILAGGSGTRLYPVTMAVSQQLLPIYDKPMIYYPLSTLMLAGIR
DILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFI
GHDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVE
FDQAGTAVSLEEKPLQPKSNYAVTGLFFYDNSVVEMAKNLKPSARGELEI
TDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLK
VSCPEEIAFRKNFINAQQVIELAGPLSKNDYGKYLLKMV
3D structure
PDB1mp5 Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineering
ChainD
Resolution2.75 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 G12 Q83 P86 D87 G88 L89 L109 D111 Y146 G147 E162 K163 V173 R195 I200 T201 W224 L9 G11 G12 Q83 P86 D87 G88 L89 L109 D111 Y146 G147 E162 K163 V173 R195 I200 T201 W224
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:1mp5, PDBe:1mp5, PDBj:1mp5
PDBsum1mp5
PubMed12374866
UniProtP26393|RMLA_SALTY Glucose-1-phosphate thymidylyltransferase (Gene Name=rmlA)

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