Structure of PDB 7z15 Chain I Binding Site BS02

Receptor Information
>7z15 Chain I (length=253) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSIS
ARLTPQQGEIHYENRSLYAMSEADRRRLLRTEWGVVHQHPLDGLRRQVSA
GGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQ
RLQIARNLVTHPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIV
THDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYTQLLVSSVLQN
ENL
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 chain7z15 Chain I Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7z15 Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
Resolution1.93 Å
Binding residue
(original residue number in PDB)		T45 Q90
Binding residue
(residue number reindexed from 1)		T43 Q88
Annotation score1
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0015716 organic phosphonate transport
GO:0015833 peptide transport
GO:0019634 organic phosphonate metabolic process
GO:0019700 organic phosphonate catabolic process
Cellular Component
GO:0061694 alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex
GO:1904176 carbon phosphorus lyase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7z15, PDBe:7z15, PDBj:7z15
PDBsum7z15
PubMed36813778
UniProtP16678|PHNK_ECOLI Putative phosphonates utilization ATP-binding protein PhnK (Gene Name=phnK)

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