Structure of PDB 8fdb Chain A Binding Site BS03
Receptor Information
>8fdb Chain A (length=332) Species:
318161
(Shewanella denitrificans OS217) [
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TTNTIMEQEARTAPQKIAEQLLANDAITESLGSVLREFKPKFVMIVGRGS
SDHAGVFAKYLFEIEASIPTFAAAPSVASVYGKTLKLAGGLVIVISQSGR
SPDILAQARMAKNAGAFCVALVNDETAPIKDIVDVVIPLRAGEEKAVAAT
KSYLATLSALLQVAAKWTQNESLVEAVNSLPQALQAAVDAEPQLRAGSLT
DVKNLVVLGRGFGYAVSKEIALKLKEVCAIHAEAFSSAEFLHGPVTLVEK
KLSILDVCIRDESYGSHVEQIANVKQRGANLIHLHQTSADIHPRIAPLAL
LQRFYIDVAAVAIALGINPDKPAGLKKVTQTL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
8fdb Chain A Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
8fdb
Substrate binding in the allosteric site mimics homotropic cooperativity in the SIS-fold glucosamine-6-phosphate deaminases.
Resolution
3.06 Å
Binding residue
(original residue number in PDB)
G48 R49 I96 S97
Binding residue
(residue number reindexed from 1)
G47 R48 I95 S96
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.6.1.16
: glutamine--fructose-6-phosphate transaminase (isomerizing).
Gene Ontology
Molecular Function
GO:0004360
glutamine-fructose-6-phosphate transaminase (isomerizing) activity
GO:0008483
transaminase activity
GO:0097367
carbohydrate derivative binding
Biological Process
GO:1901135
carbohydrate derivative metabolic process
Cellular Component
GO:0005737
cytoplasm
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Cellular Component
External links
PDB
RCSB:8fdb
,
PDBe:8fdb
,
PDBj:8fdb
PDBsum
8fdb
PubMed
37145875
UniProt
Q12KP2
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