Structure of PDB 2j4j Chain F Binding Site BS02

Receptor Information
>2j4j Chain F (length=226) Species: 273057 (Saccharolobus solfataricus P2) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNIILKISGKFFDEDNVDNLIVLRQSIKELADNGFRVGIVTGGGSTARRY
IKLAREIGIGEAYLDLLGIWASRLNAYLVMFSLQDLAYMHVPQSLEEFIQ
DWSHGKVVVTGGFQPGQSTAAVAALVAEASSSKTLVVATNVDGVYEKDPR
IYADVKLIPHLTTQDLRKILEGSQSVQAGTYELLDPLAIKIVERSKIRVI
VMNYRKLNRIIDILKGEEVSSIIEPV
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2j4j Chain F Residue 229 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2j4j Structural and Enzymatic Investigation of the Sulfolobus Solfataricus Uridylate Kinase Shows Competitive Utp Inhibition and the Lack of GTP Stimulation
Resolution2.1 Å
Binding residue
(original residue number in PDB)
R48 T180 Y181
Binding residue
(residue number reindexed from 1)
R48 T180 Y181
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.4.22: UMP kinase.
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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Cellular Component
External links
PDB RCSB:2j4j, PDBe:2j4j, PDBj:2j4j
PDBsum2j4j
PubMed17297917
UniProtQ97ZE2|PYRH_SACS2 Uridylate kinase (Gene Name=pyrH)

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