Structure of PDB 5f2v Chain T Binding Site BS02

Receptor Information
>5f2v Chain T (length=195) Species: 1415167 (Bacillus subtilis PY79) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DKQWERFLVPYRQAVEELKVKLKGIRTLYEYEDDHSPIEFVTGRVKPVAS
ILEKARRKSIPLHEIETMQDIAGLRIMCQFVDDIQIVKEMLFARKDFTVV
DQRDYIAEHKESGYRSYHLVVLYPLQTVSGEKHVLVEIQIRTLAMNFWAT
IEHSLNYKYSGNIPEKVKLRLQRASEAASRLDEEMSEIRGEVQEA
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 chain5f2v Chain T Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5f2v Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		D72 E139
Binding residue
(residue number reindexed from 1)		D70 E137
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.6.5: GTP diphosphokinase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0008728 GTP diphosphokinase activity
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0015969 guanosine tetraphosphate metabolic process
GO:0015970 guanosine tetraphosphate biosynthetic process
GO:0016310 phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5f2v, PDBe:5f2v, PDBj:5f2v
PDBsum5f2v
PubMed26460002
UniProtO31611|YJBM_BACSU GTP pyrophosphokinase YjbM (Gene Name=yjbM)

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