Structure of PDB 5f2v Chain Z

Receptor sequence
>5f2vZ (length=179) Species: 1415167 (Bacillus subtilis PY79) [Search protein sequence]
QWERFLVPYRQAVEELKVKLKGIRTLYEYEDDHSPIEFVTGRVKPVASIL
EKARRKSIPLHEIETMQDIAGLRIMCQFVDDIQIVKEMLFARKDFTVVRS
YHLVVLYPLQTVSGEKHVLVEIQIRTLAMNFWATIEHSLNYKYSGNIPEK
VKLRLQRASEAASRLDEEMSEIRGEVQEA
3D structure
PDB5f2v Catalytic mechanism and allosteric regulation of an oligomeric (p)ppGpp synthetase by an alarmone.
ChainZ
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.6.5: GTP diphosphokinase.
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 APC Z R43 K45 S49 K53 D69 L73 R74 Q138 H152 R42 K44 S48 K52 D68 L72 R73 Q123 H137
BS02 MG Z D69 E136 D68 E121
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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