Structure of PDB 1h5r Chain B

Receptor sequence
>1h5rB (length=290) Species: 562 (Escherichia coli) [Search protein sequence]
KMRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRD
ILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQPSPDGLAQAFIIGEEFIG
GDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEF
DKNGTAISLEEKPLEPKSNYAVTGLYFYDNDVVQMAKNLKPSARGELEIT
DINRIYLEQGRLSVALMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKV
SCPEEIAFRKGFIDVEQVRKLAVPLIKNNYGQYLYKQTKD
3D structure
PDB1h5r Kinetic and Crystallographic Analyses Support a Sequential-Ordered Bi Bi Catalytic Mechanism for Escherichia Coli Glucose-1-Phosphate Thymidylyltransferase
ChainB
Resolution1.9 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 THM B F114 Y115 G116 L119 S252 F113 Y114 G115 L118 S251
BS02 THM B L9 G11 G12 Q83 P86 G88 L89 D111 L8 G10 G11 Q82 P85 G87 L88 D110
BS03 G1P B Y146 G147 E162 V173 R195 Y145 G146 E161 V172 R194
Gene Ontology
Molecular Function
GO:0008879 glucose-1-phosphate thymidylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0042802 identical protein binding
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
GO:0051289 protein homotetramerization
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1h5r, PDBe:1h5r, PDBj:1h5r
PDBsum1h5r
PubMed11697907
UniProtP37744|RMLA1_ECOLI Glucose-1-phosphate thymidylyltransferase 1 (Gene Name=rfbA)

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