Structure of PDB 1g1l Chain E

Receptor sequence

>1g1lE (length=292) Species: 287 (Pseudomonas aeruginosa)

KRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIREI
LIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIGN
DLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEFD
QGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEITD
VNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKVA
CPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY

3D structure

• PDB: 1g1l The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
• Chain: E
• Resolution: 1.77 Å

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	DAU	E	L8 G10 G11 Q26 Q82 P85 G87 L88 L108 D110 Y145 G146 E161 K162 V172 W223	L7 G9 G10 Q25 Q81 P84 G86 L87 L107 D109 Y144 G145 E160 K161 V171 W222
BS02	DAU	E	Y114 G115 H116 D117 F118 H119 E120 V250 E255 I256 Y293	Y113 G114 H115 D116 F117 H118 E119 V249 E254 I255 Y292
BS03	DAU	E	I216 G218 R219 G220	I215 G217 R218 G219

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

External links

• PDB: RCSB:1g1l, PDBe:1g1l, PDBj:1g1l
• PDBsum: 1g1l
• PubMed: 11118200
• UniProt: Q9HU22