Structure of PDB 2jjx Chain C

Receptor sequence
>2jjxC (length=244) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
RPYKRVLIKLSGGALADQTGNSFNSKRLEHIANEILSIVDLGIEVSIVIG
GGNIFRGHLAEEWGIDRVEADNIGTLGTIINSLMLRGVLTSKTNKEVRVM
TSIPFNAVAEPYIRLRAVHHLDNGYIVIFGGGNGQPFVTTDYPSVQRAIE
MNSDAILVAKQGVDGVFTSDPKHNKSAKMYRKLNYNDVVRQNIQVMDQAA
LLLARDYNLPAHVFNFDEPGVMRRICLGEHVGTLINDDASLLVH
3D structure
PDB2jjx The Crystal Structure of Ump Kinase from Bacillus Anthracis (Ba1797) Reveals an Allosteric Nucleotide-Binding Site.
ChainC
Resolution2.82 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.4.22: UMP kinase.
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 ATP C I114 R117 H120 I113 R116 H119
BS02 ATP C R99 N107 A108 A110 E111 R117 R98 N106 A107 A109 E110 R116
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0009041 UMP/dUMP kinase activity
GO:0016301 kinase activity
GO:0033862 UMP kinase activity
Biological Process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006225 UDP biosynthetic process
GO:0016310 phosphorylation
GO:0044210 'de novo' CTP biosynthetic process
GO:0046940 nucleoside monophosphate phosphorylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2jjx, PDBe:2jjx, PDBj:2jjx
PDBsum2jjx
PubMed18625239
UniProtA0A6L7HKK4

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