Structure of PDB 1g23 Chain H

Receptor sequence
>1g23H (length=292) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
KRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIREI
LIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIGN
DLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEFD
QGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEITD
VNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKVA
CPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY
3D structure
PDB1g23 The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA).
ChainH
Resolution2.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 G1P H L88 Y145 G146 E161 K162 L87 Y144 G145 E160 K161
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1g23, PDBe:1g23, PDBj:1g23
PDBsum1g23
PubMed11118200
UniProtQ9HU22

[Back to BioLiP]