Structure of PDB 5zdn Chain A Binding Site BS03
Receptor Information
>5zdn Chain A (length=192) Species:
1906
(Streptomyces fradiae) [
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SFAFGAVVERRDELDGRPWISYPVRVVADTPELVAVHLSHGTRLTFGDDP
FSWGPHPWQLFGDRWQSAGILQLHRPGRGHSVWVLRDADTGAFREWYVNV
EAPWRRTPTGFSTLDHEIDLVVPADSRTFRWKDVEKFEERARIGHFSPEE
ATAIRAEAADVAREIAAGEQWWDTRWSRWEPPAGWNALLQSF
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
5zdn Chain A Residue 303 [
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Receptor-Ligand Complex Structure
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PDB
5zdn
Biochemical and Structural Analysis of FomD That Catalyzes the Hydrolysis of Cytidylyl ( S)-2-Hydroxypropylphosphonate in Fosfomycin Biosynthesis.
Resolution
2.02 Å
Binding residue
(original residue number in PDB)
N109 D125 D129
Binding residue
(residue number reindexed from 1)
N99 D115 D119
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.6.1.-
Gene Ontology
Molecular Function
GO:0016787
hydrolase activity
GO:0046872
metal ion binding
Biological Process
GO:0017000
antibiotic biosynthetic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:5zdn
,
PDBe:5zdn
,
PDBj:5zdn
PDBsum
5zdn
PubMed
30010320
UniProt
D2SNF7
|FOMD_STRFR Cytidylyl-2-hydroxypropylphosphonate hydrolase (Gene Name=fomD)
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