Structure of PDB 5zdn Chain A

Receptor sequence
>5zdnA (length=192) Species: 1906 (Streptomyces fradiae) [Search protein sequence]
SFAFGAVVERRDELDGRPWISYPVRVVADTPELVAVHLSHGTRLTFGDDP
FSWGPHPWQLFGDRWQSAGILQLHRPGRGHSVWVLRDADTGAFREWYVNV
EAPWRRTPTGFSTLDHEIDLVVPADSRTFRWKDVEKFEERARIGHFSPEE
ATAIRAEAADVAREIAAGEQWWDTRWSRWEPPAGWNALLQSF
3D structure
PDB5zdn Biochemical and Structural Analysis of FomD That Catalyzes the Hydrolysis of Cytidylyl ( S)-2-Hydroxypropylphosphonate in Fosfomycin Biosynthesis.
ChainA
Resolution2.02 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.6.1.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CDP A W68 F71 W75 Q76 S77 K142 W58 F61 W65 Q66 S67 K132
BS02 MG A E127 D129 D143 E117 D119 D133
BS03 MG A N109 D125 D129 N99 D115 D119
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:5zdn, PDBe:5zdn, PDBj:5zdn
PDBsum5zdn
PubMed30010320
UniProtD2SNF7|FOMD_STRFR Cytidylyl-2-hydroxypropylphosphonate hydrolase (Gene Name=fomD)

[Back to BioLiP]