Structure of PDB 3pkp Chain B

Receptor sequence
>3pkpB (length=289) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium) [Search protein sequence]
KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRD
ILIISTPQDTPRFQQLLGDGSQWGLNLQYKVSPSPDGLAQAFIIGEEFIG
HDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEF
DQKGTAVSLEEKPLQPKSNYAVTGLYFYDNSVVEMAKNLKPSARGELEIT
DINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIEERQGLKV
SCPEEIAFRKNFINAQQVIELAGPLSKNDYGKYLLKMVK
3D structure
PDB3pkp Expanding the Nucleotide and Sugar 1-Phosphate Promiscuity of Nucleotidyltransferase RmlA via Directed Evolution.
ChainB
Resolution2.6 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 DTP B G11 G12 S13 G14 T15 R16 K26 Q27 S83 P86 G110 D111 G10 G11 S12 G13 T14 R15 K25 Q26 S82 P85 G109 D110
BS02 MG B D111 D226 D110 D225
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3pkp, PDBe:3pkp, PDBj:3pkp
PDBsum3pkp
PubMed21317292
UniProtP26393|RMLA_SALTY Glucose-1-phosphate thymidylyltransferase (Gene Name=rmlA)

[Back to BioLiP]