Structure of PDB 7txg Chain B Binding Site BS02

Receptor Information
>7txg Chain B (length=328) Species: 263 (Francisella tularensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNRKVALEAVRVTELAALASWSQMGRGDKIAADQAAVDAMRKALNEVDID
GTVVIGEGELDEAPMLYIGEKVGAGGCEVDIALDPLEGTTITSKGGANAL
TVLAMADKGGFLNAPDVYMQKIAVGGINAPKGIVDLDDSVTNNLKRIAEF
KGVHMSALVVCTMDRPRHEHIIKEARECGARVILINDGDVSGVIATATEN
SGIDVYIGTGGAPEGVLAAAALKCLGGQMQARLIFNDEEEIKRAHRLGIT
DLNKKYDIDDLASGDIVFAATGVTDGNMLQGVKRVNSTRRGSYAVTHSVV
MRSTTKTVRHITAEHSFDFKEGIEKFMS
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain7txg Chain B Residue 406 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7txg New structures of Class II Fructose-1,6-Bisphosphatase from Francisella tularensis provide a framework for a novel catalytic mechanism for the entire class.
Resolution1.9 Å
Binding residue
(original residue number in PDB)
D84 L86
Binding residue
(residue number reindexed from 1)
D84 L86
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006071 glycerol metabolic process
GO:0006094 gluconeogenesis
GO:0030388 fructose 1,6-bisphosphate metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7txg, PDBe:7txg, PDBj:7txg
PDBsum7txg
PubMed37352301
UniProtQ5NEJ8

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