BioLiP

Structure of PDB 3pkq Chain C

Receptor sequence

>3pkqC (length=284) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]

RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIL
IISTPQDTPRFQQLLGDGSQWGLNLQYKVDPSPDGLAQAFIIGEEFIGHD
DCALVLGDNIFYGHDLPKLMEAAVNKSGATVFAYHVNDPERYGVVEFDQK
GTAVSLEEKPLQPKSNYAVTGLYFYDNSVVEMAKNLKPSAELEITDINRI
YMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKVSCPEE
IAFRKNFINAQQVIELAGPLSKNDYGKYLLKMVK

3D structure

PDB

3pkq Expanding the Nucleotide and Sugar 1-Phosphate Promiscuity of Nucleotidyltransferase RmlA via Directed Evolution.

Chain

Resolution

2.4 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	DGT	C	L9 G11 G12 S13 G14 T15 R16 Q27 I55 D83 S85 L109 G110 D111	L6 G8 G9 S10 G11 T12 R13 Q24 I52 D80 S82 L106 G107 D108
BS02	MG	C	D111 D226	D108 D220

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0008879	glucose-1-phosphate thymidylyltransferase activity
GO:0016779	nucleotidyltransferase activity
GO:0046872	metal ion binding

	Biological Process
GO:0009058	biosynthetic process
GO:0009103	lipopolysaccharide biosynthetic process
GO:0009243	O antigen 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

PDB	RCSB:3pkq, PDBe:3pkq, PDBj:3pkq
PDBsum	3pkq
PubMed	21317292
UniProt	P26393\|RMLA_SALTY Glucose-1-phosphate thymidylyltransferase (Gene Name=rmlA)