Structure of PDB 5zdm Chain A Binding Site BS02

Receptor Information
>5zdm Chain A (length=198) Species: 1906 (Streptomyces fradiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ESFAFGAVVERRDELDGRPWISYPVRVVADTPELVAVHLSHGTRLTFGDD
PFSWGPHPWQLFGDRWQSAGILQLHRPGRGHSVWVLRDADTGAFREWYVN
VEAPWRRTPTGFSTLDHEIDLVVPADSRTFRWKDVEKFEERARIGHFSPE
EATAIRAEAADVAREIAAGEQWWDTRWSRWEPPAGWNALLQSFETEGS
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain5zdm Chain A Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5zdm Biochemical and Structural Analysis of FomD That Catalyzes the Hydrolysis of Cytidylyl ( S)-2-Hydroxypropylphosphonate in Fosfomycin Biosynthesis.
Resolution1.38 Å
Binding residue
(original residue number in PDB)
E127 D129 D143
Binding residue
(residue number reindexed from 1)
E118 D120 D134
Annotation score1
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5zdm, PDBe:5zdm, PDBj:5zdm
PDBsum5zdm
PubMed30010320
UniProtD2SNF7|FOMD_STRFR Cytidylyl-2-hydroxypropylphosphonate hydrolase (Gene Name=fomD)

[Back to BioLiP]