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BioLiP

Structure of PDB 2j4j Chain B Binding Site BS03

Receptor Information
>2j4j Chain B (length=216) 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
IYADVKLIPHLTTQDLRKILEELLDPLAIKIVERSKIRVIVMNYRKLNRI
IDILKGEEVSSIIEPV
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain2j4j Chain B Residue 230 [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)		Y88 H104
Binding residue
(residue number reindexed from 1)		Y88 H104
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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Biological Process
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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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