Structure of PDB 1fxo Chain D

Receptor sequence
>1fxoD (length=292) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
KRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIREI
LIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIGN
DLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEFD
QGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEITD
VNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKVA
CPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY
3D structure
PDB1fxo The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
ChainD
Resolution1.66 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 TMP D G218 R219 G220 G217 R218 G219
BS02 TMP D L8 G10 G11 Q26 Q82 P85 G87 L88 D110 L7 G9 G10 Q25 Q81 P84 G86 L87 D109
BS03 TMP D Y114 G115 H116 D117 E255 I256 Y113 G114 H115 D116 E254 I255
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008879 glucose-1-phosphate thymidylyltransferase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009058 biosynthetic process
GO:0009244 lipopolysaccharide core region 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:1fxo, PDBe:1fxo, PDBj:1fxo
PDBsum1fxo
PubMed11118200
UniProtQ9HU22

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