Structure of PDB 1g1l Chain B

Receptor sequence

>1g1lB (length=293) Species: 287 (Pseudomonas aeruginosa)

MKRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIRE
ILIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIG
NDLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEF
DQGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEIT
DVNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKV
ACPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY

3D structure

• PDB: 1g1l The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
• Chain: B
• 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	B	L8 G10 Q26 Q82 P85 G87 L88 L108 D110 Y145 G146 E161 K162 V172	L8 G10 Q26 Q82 P85 G87 L88 L108 D110 Y145 G146 E161 K162 V172
BS02	DAU	B	Y114 G115 H116 D117 F118 H119 E120 V250 E255 I256 R259 Y293	Y114 G115 H116 D117 F118 H119 E120 V250 E255 I256 R259 Y293
BS03	DAU	B	I216 G218 R219 G220	I216 G218 R219 G220

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