Structure of PDB 1mc3 Chain A

Receptor sequence
>1mc3A (length=291) Species: 562 (Escherichia coli) [Search protein sequence]
HMKGIILAGGSGTRLHPITRGVSKQLLPIYDKPMIYYPLSVLMLAGIREI
LIITTPEDKGYFQRLLGDGSEFGIQLEYAEQPSPDGLAQAFIIGETFLNG
EPSCLVLGDNIFFGQGFSPKLRHVAARTEGATVFGYQVMDPERFGVVEFD
DNFRAISLEEKPKQPKSNWAVTGLYFYDSKVVEYAKQVKPSERGELEITS
INQMYLEAGNLTVELLGRGFAWLDTGTHDSLIEASTFVQTVEKRQGFKIA
CLEEIAWRNGWLDDEGVKRAASSLAKTGYGQYLLELLRARP
3D structure
PDB1mc3 Crystal Structure of Escherichia coli Glucose-1-Phosphate Thymidylyltransferase (RffH) Complexed with dTTP and Mg2+
ChainA
Resolution2.6 Å
3D
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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 MG A D108 D223 D109 D224
BS02 TTP A L6 G8 G9 G11 T12 R13 K23 Q24 Q80 P83 L86 D108 L7 G9 G10 G12 T13 R14 K24 Q25 Q81 P84 L87 D109
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008879 glucose-1-phosphate thymidylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0000271 polysaccharide biosynthetic process
GO:0009058 biosynthetic process
GO:0009243 O antigen biosynthetic process
GO:0009246 enterobacterial common antigen biosynthetic process
GO:0045226 extracellular polysaccharide biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:1mc3, PDBe:1mc3, PDBj:1mc3
PDBsum1mc3
PubMed12171937
UniProtP61887|RMLA2_ECOLI Glucose-1-phosphate thymidylyltransferase 2 (Gene Name=rffH)

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