Structure of PDB 7z15 Chain G Binding Site BS01
Receptor Information
>7z15 Chain G (length=353) Species:
562
(Escherichia coli) [
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MYVAVKGGEKAIDAAHALQESRRRGDTDLPELSVAQIEQQLNLAVDRVMT
EGGIADRELAALALKQASGDNVEAIFLLRAYRTTLAKLAVSEPLDTTGMR
LERRISAVYKDIPGGQLLGPTYDYTHRLLDFTLLANGEAPTLTTADSEQQ
PSPHVFSLLARQGLAKFEEDSGAQPDDITRTPPVYPCSRSSRLQQLMRGD
EGYLLALAYSTQRGYGRNHPFAGEIRSGYIDVSIVPEELGFAVNVGELLM
TECEMVNGFIDPPDEPPHFTRGYGLVFGMSERKAMAMALVDRALQAPEYG
EHATGPAQDEEFVLAHADNVEAAGFVSHLKLPHYVDFQAELELLKRLQQE
KNH
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
7z15 Chain G Residue 1000 [
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Receptor-Ligand Complex Structure
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PDB
7z15
Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
Resolution
1.93 Å
Binding residue
(original residue number in PDB)
H328 H333
Binding residue
(residue number reindexed from 1)
H328 H333
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.7.8.37
: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase.
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0016740
transferase activity
GO:0061693
alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity
Biological Process
GO:0015716
organic phosphonate 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
PDBsum
7z15
PubMed
36813778
UniProt
P16687
|PHNI_ECOLI Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI (Gene Name=phnI)
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