Structure of PDB 3zlk Chain D

Receptor sequence
>3zlkD (length=293) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
MKRKGIILAGGSGTRLHPATLAISKQLLPVYDKPMIYYPLSTLMLAGIRE
ILIISTPQDTPRFQQLLGDGSNWGLDLQYAVQPSPDGLAQAFLIGESFIG
NDLSALVLGDNLYYGHDFHELLGSASQRQTGASVFAYHVLDPERYGVVEF
DQGGKAISLEEKPLEPKSNYAVTGLYFYDQQVVDIARDLKPSPRGELEIT
DVNRAYLERGQLSVEIMGRGYAWLDTGTHDSLLEAGQFIATLENRQGLKV
ACPEEIAYRQKWIDAAQLEKLAAPLAKNGYGQYLKRLLTETVY
3D structure
PDB3zlk Allosteric competitive inhibitors of the glucose-1-phosphate thymidylyltransferase (RmlA) from Pseudomonas aeruginosa.
ChainD
Resolution1.952 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 Y46 D S41 L45 Y113 Y114 G115 V250 A251 E255 S41 L45 Y113 Y114 G115 V250 A251 E255 MOAD: ic50=1.32uM
BindingDB: IC50=1.32e+3nM
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:3zlk, PDBe:3zlk, PDBj:3zlk
PDBsum3zlk
PubMed23138692
UniProtQ9HU22

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