Structure of PDB 4lzz Chain L Binding Site BS03

Receptor Information
>4lzz Chain L (length=246) Species: 63363 (Aquifex aeolicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YVFESPKMKEILEKIKKISCAECPVLITGESGVGKEVVARLIHKLSDRSK
EPFVALNVASIPRDIFEAELFGYEKGAFTGAVSSKEGFFELADGGTLFLD
EIGELSLEAQAKLLRVIESGKFYRLGGRKEIEVNVRILAATNRNIKELVK
EGKFREDLYYRLGVIEIEIPPLRERKEDIIPLANHFLKKFSRKYAKEVEG
FTKSAQELLLSYPWYGNVRELKNVIERAVLFSEGKFIDRGELSCLV
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 chain4lzz Chain L Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4lzz Nucleotide-induced asymmetry within ATPase activator ring drives sigma 54-RNAP interaction and ATP hydrolysis.
Resolution3.21 Å
Binding residue
(original residue number in PDB)		E174 D238
Binding residue
(residue number reindexed from 1)		E36 D100
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008134 transcription factor binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0006355 regulation of DNA-templated transcription

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4lzz, PDBe:4lzz, PDBj:4lzz
PDBsum4lzz
PubMed24240239
UniProtO67198

[Back to BioLiP]