Structure of PDB 5zwk Chain D Binding Site BS03

Receptor Information
>5zwk Chain D (length=319) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYG
IAGVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVC
FDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYAL
YGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPA
NKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPV
ILGSPDDVLEFLKVYEKHS
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 chain5zwk Chain D Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5zwk Location of FBPase catalytic metal binding site: a combined experimental and theoretical study
Resolution2.104 Å
Binding residue
(original residue number in PDB)
E97 D118 L120
Binding residue
(residue number reindexed from 1)
E81 D102 L104
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016787 hydrolase activity
GO:0016791 phosphatase activity
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0042578 phosphoric ester hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006094 gluconeogenesis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5zwk, PDBe:5zwk, PDBj:5zwk
PDBsum5zwk
PubMed
UniProtQ2TU34

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